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					XXI ICMRBS THE SCIENTIFIC PROGRAMME SUNDAY, January 16 4:00-6:30 pm Sunday afternoon INAUGURAL SESSION, Hall A Chairpersons: Edwin D Becker & Girjesh Govil NMR and its Nobel Glory: Richard R. Ernst, Laboratorium für Physikalische Chemie ETH Hönggerberg HCI 8093 Zürich, Switzerland The Evolution of the NMR View of Biological Macromolecules: Kurt Wuthrich1 Dept. of Molecular Biology, The Scripps Research Institute (TSRI), La Jolla, CA Institut fur Molekularbiologie and Biophysik, Eidgenossiche Technische Hochschule (ETH) Zurich, CH-8093 Zurich, Switzerland Which aspects of brain function does fMRI measure?: Seiji Ogawa, Hamano Life Science research Foundation, Ogawa Laboratories for Brain Function Research, Shinjuku-ku, Tokyo, 160-0015, Japan CULTURAL PROGRAM, Hall A WELCOME DINNER, Mountain Heights, Shilpakala Vedika MONDAY, January 17 8:30-9:00 am POSTER SET-UP, Halls D & E Display your posters at the space mentioned in the program. Monday morning PLENARY SESSION, Hall A Chairpersons: Ivano Bertini & Anil Kumar NMR Spectroscopy in Studies of Protein Folding and Misfolding: C. M. Dobson, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW Understanding global systems biology via NMR spectroscopy and metabonomics: Jeremy K. Nicholson, Biological Chemistry, Imperial College, London University, London SW7 2AZ UK BREAK (Tea), Shilpakala Vedika Lawns Monday morning parallel session A Proteomics, Hall A Chairpersons: John Markley & P T Manoharan Membrane Protein Structural Biology and Structural Genomics: T. A. Cross1,2, F. P. Gao1,2, W. Brey1, P. GorÕkov1, E. Chekmenev1, K. Taylor2, R.K. Nakamoto3, C. R. Sanders4 , F. Sonnichsen5, S. J. Opella6 et al, 1 National High Magnetic Field Laboratory, Tallahassee, FL 32310, USA, 2 Florida State University, Tallahassee, FL 32306, USA, 3University of Virginia, Charlottesville, VA, USA, 4Vanderbilt University, Nashville, TN 37232-8725 USA, 5Case Western Reserve University, Cleveland, OH 41406-4970, USA, 6 University of California, San Diego, CA 92093-0307 USA

Inaugural 4:15 pm

Inaugural 5:00 pm

Inaugural 5.45 pm

6:30-7:15 pm 7:30-9:00 pm

9:00-10:30 am

Plenary 9:00 am

Plenary 9:45 am

10:30-11:00 am 11:00-01:00 am

MOA 11:00 am

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The role of NMR in structural genomics: from gene to the biological function of metalloproteins: Lucia Banci, Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy NMR-Based Structural Genomics at the Pacific Northwest National Laboratory: Michael A. Kennedy, Pacific Northwest National Laboratory, Biological Sciences Division, EMSL 2569, K8-98, Richland, WA 99352 USA Structural Proteomics of Eukaryotic Protein Domain Families: G. V. T. Swapna, T. Acton, R. Shastry, Y. Chiang, J. Huang, H. Moseley, Gaetano T,Montelione, Center for Advanced Biotechnology Medicine, Northeast Structural Genomics Consortium, Rutgers University, Piscataway, NJ 08854 Monday morning parallel session B SS NMR-I, Hall B Chairpersons: H Akutsu & S Ganapaty Double-Quantum Solid-State NMR of the Rhodopsin Chromophore: Wai Cheu Lai1, Luminita Duma2, Marina Carravetta1, Ole G. Johannessen1, Michiel A. Verhoeven3, Petra H. M. Bovee-Geurts4, Johan Lugtenburg3, Willem J. deGrip4, Lyndon Emsley2, Steven P. Brown5, and Malcolm H. Levitt1, 1School of Chemistry, University of Southampton, UK, 2Laboratoire de Chimie, ENSLyon, France, 3Leiden Institute of Chemistry, Leiden University, The Netherlands, 4Nijmegen Center for Molecular Life Sciences, University of Nijmegen Medical School, The Netherlands, 5Department of Physics, University of Warwick, UK Structural Studies of Antimicrobial Peptides Using Solid-State NMR: Ayyalusamy Ramamoorthy, S. Thennarasu, K. Yamamoto, T. Narasimhaswamy, D. K. Lee, K. A. H. Henzler-Wildman, and K. J. Hallock, Biophysics Research Division and Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055 Structural Analysis of Membrane-Bound Peptide Mastoparan-X by SolidState NMR under Magic-Angle Spinning: Toshimichi Fujiwara and Hideo Akutsu, Institute for Protein Research, Osaka University, Japan Investigation of uniformly 13C/15N labeled alpha-Synuclein Fibrils with Multidimensional MAS Solid-State NMR: H. Heise,1 W. Hoyer,1 S. Becker,1 V. Subramaniam,1 T.M. Jovin,1 M. Baldus1, 1Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany Novel Solid-State NMR Approach to Structural Analysis of Proteins: Application to Phoborhodopsin Transducer pHtrII in Lipid Membrane Environment: Yoh Matsuki,1,4 Yuki Sudo,2 Chojiro Kojima,3 Toshimichi Fujiwara,4 Naoki Kamo,2 Hideo Akutsu,4 1JST-BIRD,2Graduate School of Pharmaceutical Science, Hokkaido University,3Graduate School of Biological Science, Nara Institute for Science and Technology, 4Institute for Protein Research, Osaka University Phase modulated Lee-Goldberg sequence and proton spectroscopy in solidstate: P. K. Madhu, Elena Vinogradov, Leon Bosman, and Shimon Vega, Department of Chemical Sciences, Tata Institute of Fundamental Research, Colaba, Mumbai 400 005, India, Department of Chemical Physics, Weizmann Institute of Science, Rehovot 76100, Israel

MOA 12:00 pm

MOA 12:30 pm

11:00-01:15 am

MOB 11:00 am

MOB 11:30 am

MOB 12:00 pm

MOB 12:30 pm

MOB 12:45 pm

MOB 01:00 pm

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Monday morning parallel session C Methods-I Hall C Chairpersons: Pattrick Cozzone & N Jagannathan High Resolution Brain MRI using a 4.7 T Magnet: Ordidge RJ, Thomas D, Parkes H and Turner R, University College London Determine peptide plane orientation using residual dipolar coupling: Joseph D. Walsh1, John Kuszewski2 and Yun-Xing Wang1, 1Protein Nucleic Acid Interaction Section, Structural Biophysics Laboratory,NCI-Frederick, NIH, Frederick, MD 21702, 2Imaging Sciences Lab, Division of Computational Biology, CIT, NIH, Bethesda, MD 20892 Measurement of cerebral perfusion using bolus contrast MRI: Fernando Calamante, Institute of Child Health,University College London, UK In-Cell NMR studies of various proteins expressed in E. coli: Masatoshi Yoshimasu,1,2 Tsutomu Mikawa,2,3,4 Nobuhiro Hayashi,5 Takehiko Shibata,1,3,4 and Yutaka Ito2,3,4 1Cellular and Molecular Biology Laboratory and 3Research Group of Bio-supramolecular Structure-Function, RIKEN, JAPAN; 2 CREST/JST; 4Graduate School of Integrated Science, Yokohama-City University, JAPAN; 5Fujita Health University, JAPAN Novel Probes for Magnetic Resonance Imaging: A. Manivannan1 and S. Sendhil Velan2, 1Physics Department, 2Center for Advanced imaging and Radiology West Virginia University, Morgantown, WV 26506, USA LUNCH BREAK Sampradaya POSTER SESSION and EXHIBITS, Halls D & E (with tea and cookies) Odd numbered posters are discussed during this time Monday afternoon parallel session A Paramagnetic Proteins, Hall A Chairpersons: Lucia Banci & B D N Rao

MOC 11:00 am MOC 11:30 am

MOC 12:00 pm

MOC 12:30 pm

MOC 12:45 pm

01:15-02:00 pm 02:00-04:00 pm

04:00-06:15 pm

MOA 4:00 pm

Paramagnetic Labelling of Proteins for Biomolecular NMR: Gottfried Otting1, Guido Pintacuda1,2, Thomas Huber3, Max A. Keniry1, XunCheng Su1, Ah Young Park1, Nicholas E. Dixon1, Ahmad Moshref2, Ainars Leonchiks4, Anatoly Sharipo4, Andrei Kaikkonen2, 1 Australian National University, Canberra, ACT 0200, Australia, 2 Karolinska Institute, S-17177 Stockholm, Sweden, 3 The University of Queensland, Department of athematics, Brisbane QLD 4072, Australia, 4 University of Latvia, LV-1067 Riga, Latvia New Insights into STAT Tetramerization Derived from the Solution Structure of the N-terminal Domain of STAT4: Vadim Gaponenko, Amanda S. Altieri, Jess Li, Sergey Tarasov, R. Andrew Byrd, Structural Biophysics Laboratory, National Cancer Institute, Frederick, MD 21702

MOA 4:30 pm

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Energetics and Mechanism of Ca2+ displacement by lanthanides in a calcium binding protein: K.V.R. Chary, Department of Chemical Sciences, Tata Institute of Fundamental Research, Mumbai 400 005 NMR studies of copper (II) interacting with peptides derived from the prion and the amyloid precursor proteins: Elena Gaggelli, Daniela Valensin and Gianni Valensin, Department of Chemistry, University of Siena, Via Aldo Moro, Siena 53100, Italy Roles of Noncoordinated Aromatic Residues in Redox Regulation of Cytochrome c3 from Desulfovibrio vulgaris Miyazaki F: Yuki Takayama1, Erisa Harada1,2, Rie Kobayashi3, Kiyoshi Ozawa3, and Hideo Akutsu1,1Institute for Protein Research, Osaka University, Yamadaoka, Suita 565-0871, Japan, Japan 2Biological Informatics Consortium, Chuo-ku, Tokyo 104-0032, Japan, and Faculty of Engineering, 3Yokohama National University, Hodogaya-ku, Yokohama 240-8501, Japan Structural basis for the observed magnetic anisotropic tensorial values in a calcium binding protein: Sourajit M. Mustafi, Sulakshana Mukherjee and Kandala V.R Chary, Department of Chemical Sciences, Tata Institute of Fndamental Research, Mumbai 400005 Monday afternoon parallel session B MR Imaging-I Hall, B Chairpersons: Zaver M Bhujwalla & R P Tripathi Ultra fast and parallel imaging: J. Hennig, University Hospital Freiburg, Germany Direct and indirect detection of tissue protein and peptides in vivo using exchangeable amide protons: Peter van Zijl and Jinyuan Zhou, Johns Hopkins University Medical School, Dept. of Radiology, Div. of MRI Research, Baltimore, MD 21205, F.M. Kirby Research Center for Functional Brain Imaging, Kennedy Krieger Institute, Baltimore, MD 21205

MOA 5.30 pm

MOA 5:45 pm

MOA 6:00 pm

04:00-06:15 pm

MOB 4:00 pm

MOB 4:30 pm

MOB 5:00 pm

Potential of various in vivo MR methodologies in the evaluation of cancer: Virendra Kumar, Uma Sharma, KA Danishad and N.R. Jagannathan, Department of NMR, All India Institute of Medical Sciences, New Delhi, India Investigation of Muscle Metabolism by Multi-Dimensional Localized Magnetic Resonance Spectroscopic Techniques at 3T: S. Sendhil Velan1, Susan Lemieux1, Raymond R. Raylman1, M. Albert Thomas2,1Center for Advanced Imaging and Department of Radiology, West Virginia University2Department of Radiology, University of California, Los Angeles Activation of the Brain Center Associated with Visually Evoked Sexual Arousal: Functional MR Imaging: Gwang Woo Jeong, Heoung Keun Kang, Hyung Joong Kim, Hyeong Jung Kim, Jeong Jin Seo, Department of Radiology, Chonnam National University Medical School, Gwangju 501-190, Korea

MOB 5:30 pm

MOB 5:45 pm

04:00-06:15 pm

Monday afternoon parallel session C Nucleic Acid Structures-I, Hall C Chairpersons: G Varani & R V Hosur

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MOC 4:00 pm

Molecular recognition during spliceosome assembly and RNA interference: M. Sattler, EMBL Heidelberg, Germany No proton - No problem: Non-protonated Nuclei in NMR Studies of Nucleic Acids: V. Sklenár, R. Fiala, and M. Munzarová ,Masaryk University Brno, Czech Republic U6 RNA Structure and Function: Samuel Butcher, Department of Biochemistry, University of Wisconsin, Madison, Madison, USA Unusual Primer-Template Structures for Low-Fidelity DNA Polymerases: S. L. Lam and L. M. Chi, Department of Chemistry, The Chinese University of Hong Kong, Hong Kong Structure of daunomycin complexed with d-TGATCA by nuclear mangentic resonance spectroscopy and restrained molecular dynamics: Monica,1 S.K.Barthwal,2 R. Barthwal,1, 1Department of Biotechnology and 2 Physics, Indian Institute of Technology Roorkee, 247667 India TRNOE analysis of the single-stranded DNA structure induced by binding of the yeast mitochondrial DNA recombination protein Mhr1p: Tokiha Masuda1,2, Tsutomu Mikawa1,2,3,4, Masatoshi Yoshimasu3,4, Feng Ling3, Takehiko Shibata1,2,3 and Yutaka Ito1,2,3,41Molecular and Cellular Physiology Laboratory, Graduate School of Integrated Science, Yokohama City University, Japan; 2Research Group for Bio-supramolecular Structure-Function, RIKEN, Japan; 3Cellular and Molecular Biology Laboratory, RIKEN, Japan; 4 CREST/JST CULTURAL PROGRAM Hall

MOC 4:30 pm

MOC 5:00 pm

MOC 5:30 pm

MOC 6:00 pm

MOC 6:15 pm

06:15-07:45 pm A 08:00 onwards

DINNER AND FELICITATIONS TO THE HONORARY FELLOWS OF NATIONAL MAGNETIC RESONANCE SOCIETY OF INDIA, Rock Heights, Shilpakala Vedika TUESDAY, January 18

9:00-10:30 am

Tuesday morning PLENARY SESSION, Hall A Chairpersons: H J Dyson & G Bodenhausen Mapping Equilibrium Protein Folding Pathways by NMR: R. V. Hosur, Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400 005 Journey to Ultrahigh Magnetic Fields for MR imaging and spectroscopy: an increasingly sensitive probe for brain function and chemistry: Kamil Ugurbil, Center for Magnetic Resonance Research, Univ. of Minnesota Medical School, Minneapolis, MN, USA BREAK (Tea and cookies), Shilpakala Vedika

Plenary 9:00 am

Plenary 9:45 am

10:30-11:00 am Lawns 11:00-01:00 pm

Tuesday morning parallel session A Methods-II, Hall A

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Chairpersons: C Griesinger & Chandra Kumar TOA 11:00 am High pressure NMR extends protein structure and dynamics analyses to higher energy conformers: Kazuyuki Akasaka, Department of biotechnological Science, School of Biology-Oriented Science and Technology, Kinki University, 930 Nishimitani, Uchita-cho, Wakayama 649-6493, Japan Structural characterization proteins using RDCs and novel assignment strategies: 1J.H. Prestegard, Lianmei Feng, T. Weldeghiorghis, Greg Wiley, 1 Complex Carbohydrate Research Center, University of GeorgiaAthens, GA, 30602, USA GFT NMR, Progress for Rapid NMR Data Collection: T. Szyperski, State University of New York at Buffalo, Buffalo, NY 14260, USA Alignment tensor determination for a weakly-aligned protein based on orientation-induced TROSY chemical shift changes: Shin-ichi Tate,1and Hiroshi Moriuchi1, 1Biomolecular Engineering Research Institute (BERI), Osaka, Japan Sample Patterning on the Surface of Planar NMR-Microcoils: K. Ehrmann1, M. Gersbach1, P. Pascoal2, F. Vincent1, C. Massin1, D. Stamou2, P.-A. Besse1, H. Vogel2 and R.S. Popovic1, 1Institute of Microsystems, 2Institute of Chemical Sciences, EPFL – Swiss Federal Institute of Technology Lausanne, CH-1015 Lausanne, Switzerland Tuesday morning parallel session B Molecular Recognition, Hall B Chairpersons: Betty Gaffney & Javed Iqbal Structure, Function and Heparin interaction of Human Hepatoma-Derived Growth Factor-Related Proteins: Sue, S.C.1, Lee, W.T.1, Lin, Y.J.1, Chen, J.Y.1, Lee, S.C.2 Wu, W.G.2 and Huang, T.H.*,1,3, 1Inst. Biomed. Sci., Academia Sinica, Taipei; 2Inst. Bioinf. & Struct. Biol., Nat¡¦l Tsinghua U., Hsinchu; 3 Dept. Phys., Nat¡¦l Taiwan Normal U. , Taipei, Taiwan, R.O.C. NMR investigation of protein-protein and protein-ligand interactions in gene transcription and cellular signaling: Michael J. Plevin, Tapas Mal, Ivan Bosanac, Jenny Chan, Le Zheng, and Mitsu Ikura, Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 610 University Ave., Toronto, Ontario, M5G 2M9, Canada Protein:Protein Interactions Studied with Paramagnetic NMR Tools: M. Ubbink, M. Prudencio, A. N. Volkov, M. G. Finiguerra, M. D. Vlasie, Leiden Institute of Chemistry, Leiden University, The Netherlands Solution structure of the UBA domain of budding yeast DSK2p in complex with the ubiquitin: Ayako Ohno1,2, JunGoo Jee2,3, Kenichiro Fujiwara2, Takeshi Tenno2,4, Natsuko Goda2, Hidehito Tochio2, Hideki Kobayashi5, Hidekazu Hiroaki1,2 Masahiro Shirakawa2,3, 1Kihara Memorial Yokohama Foundation for the advancement of Life Sciences, Kanagawa, Japan, 2 Yokohama City University, Kanagawa, Japan, 3RIKEN GSC, Kanagawa, Japan, 4Ehime University, Ehime, Japan, 5Kyushu University, Fukuoka, Japan

TOA 11:30 am

TOA 12:00 pm

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11:00-01:15 pm

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Applications of NMR Spectroscopy and Structural Enzymology to Targetbased Discovery of Novel Antibacterials: Gunther Kern, Per-Olof Eriksson, Tomas Lundqvist, Sushmita Lahiri, Elaina Zverina, Thomas A. Keating, Brian Noonan and Gautam Sanyal*, Infection Discovery, AstraZeneca R&D Boston, 35 Gatehouse Drive, Waltham, MA 02451, USA and Structural Chemistry Laboratory, AstraZeneca R&D Mölndal, Sweden Discovery of leads for the macrophage migration inhibitory factor using fragment-based screening. A synergistic application of NMR, MS and Xray screening: C. Fernández, M.J.J. Blommers, F. Bitsch, A. Widmer, A. Marzinzik, S. Lehmann, J.-M. Rondeau Novartis Institutes for Biomedical Research, Basel, Switzerland Tuesday morning parallel session C Informatics, Education and Capacity Building, Hall C Chairpersons: K Akasaka & F Saparorich Building capacity in magnetic resonance for the future: Ian C.P. Smith, Institute for Biodiagnostics, National Research Council, Winnipeg, Canada Automation in Protein Structure Determinations: John L. Markley1,2,3, Arash Bahrami1,2,3, Claudia C. Cornilescu1,2,3, Gabriel Cornilescu1,3, Hamid Eghbalnia1,3, Klaas Hallenga1,3, Masatsune Kainosho2,5, Min S. Lee2,3, Betsy L. Lytle2,4, Carrie L. Newman2,3, Craig S. Newman1,2,3, Francis C. Peterson2,5, Mark N. Shahan2,3, Shanteri Singh2,3, Jikui Song2,3, Marco Tonelli1,3, Ejan M. Tyler2,3, Robert C. Tyler2,3, Eldon L. Ulrich1,2,3, Dmitriy A. Vinarov2,3, Brian F. Volkman2,4, Liya Wang1,2,3, William M. Westler1,2,3, Qin Zhao2,3, and Zsolt Zolnai1,2,3, 1National Magnetic Resonance Facility at Madison and 2Center for Eukaryotic Structural Genomics, 3University of Wisconsin-Madison, Madison, WI, USA, 4Medical College of Wisconsin, Milwaukee, WI, 5Tokyo Metropolitan University, Tokyo, Japan Training of Young Biological NMR Scientists in Asia: Hideo Akutsu, Institute for Protein Research, Osaka University, Suita 565-0871, Japan Activities of the Frankfurt Centre of Biomolecular MR for the Transfer of MR Knowledge: H. Rueterjans1, 1Institute of Biophysical Chemistry, J.W.Goethe University Frankfurt, Germany Education and Capacity Building in Biological NMR in Less Developed Countries: Girjesh Govil, Tata Institute of Fundamental Research, Mumbai 400 005, India LUNCH BREAK, Sampradaya Vedika POSTER SESSION and EXHIBITS, Halls D & E (with tea and cookies) Tuesday afternoon parallel session A Proteins-I, Hall A Chairpersons: G C K Roberts & S V Bhat Recent Multinuclear NMR Studies of Hemoglobin: New Insights into the Structure-Function Relationship in Hemoglobin: Chien Ho1, Carnegie Mellon University, Pennsylvania, USA

TOB 01:00 pm

11:00-01:05 pm

TOC 11:00 am

TOC 11:25 am

TOC 11:50 am

TOC 12:15 pm

TOC 12:40 pm

01:15-02:00 pm 02:00-04:00 pm

04:00-06:30 pm

TOA 4:00 pm

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TOA 4:30 pm

The structure and function of AHSP, a specific chaperone for alphahemoglobin: David A. Gell1, Chris Lee1, Suiping Zhou2, Anne Rich3, Peter Lay3, Andrew Gow2, Mitchell J. Weiss2 and Joel P. Mackay1, 1School of Molecular and Microbial Biosciences, University of Sydney, NSW, Australia 2 School of Chemistry, University of Sydney, NSW, Australia 3The Children's Hospital of Philadelphia, Philadelphia, USA Structure determination of SAP-18: insight into the structural basis of histone deacetylase specificity: Scott A. McCallum, JianPing Yin, and Wayne J. Fairbrother, Genentech Inc., California, USA The Molecular Basis of Genetic Disease caused by Single Amino Acid Residue Replacements: James A. Ferretti1, James M. Gruschus1, Kae-Jung Hwang1, Hyun-Sook Lee1, Jin-Soo Maeng1, Jeong-Ho Ju1, James W. Mack1, 1 LBC, NHLBI, NIH, Bethesda, Maryland 20892 USA Alternative Conformations of the gp120 V3 Loop suggest a mechanism for HIV-1 coreceptor selectivity and the Molecular Basis for Broad Neutralization by antibody 447-52D: Osnat Rosen, Michal Sharon and Jacob Anglister, Department of Structural Biology, The Weizmann Institute of Science, Rehovot 76100, Israel Folding Mechanism of SUMO-1: Non Native Structural characteristics of equilibrium intermediates: Ashutosh Kumar1, Sudha Srivastva1, Ram Kumar Mishra2, Rohit Mittal2, Ramkrishna V. Hosur1,1Dept. of Chemical Sciences, 2 Dept. of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai- 400005, India Tuesday afternoon parallel session B MR in Human Health and Behavior, in vivo Spectroscopy and Metabonomics, Hall B Chairpersons: Ian Smith & Sudha Srivastava NMR in Disease Diagnosis and Treatment Monitoring: C.L. Khetrapal, Center of Biomedical Magnetic Resonance, Sanjay Gandhi Post Graduate Institute of Medical Sciences, Lucknow-226 014, India Spatially Resolved Two-dimensional MR Spectroscopy in vivo: M. Albert Thomas, Department of Radiology, University of California-Los Angeles, California, USA Glucose Utilization by Normal Erythrocytes is affected by Malarial Parasite – P. falciparum infection: Haripalsingh M. Sonawat1*, Monika Mehta2#, Alfica Sehgal2, Shobhona Sharma2, 1Department of Chemical Sciences and 2 Department of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai, India. #Present address: Section of Infectious Diseases/Internal Medicine, School of Medicine, Yale University, New Haven CT 06511, USA The Regulation of GABA Synthesis during Increased Brain Activity: Anant B. Patel1, Robin A. de Graaf1, Kevin L. Behar2, Department of 1Diagnostic Radiology and 2Psychiatry, Magnetic Resonance Research Center, Yale University School of Medicine, New Haven, CT 06520, USA The hetero-nuclear NMR-based metabol(n)omics of plant and animal systems: Jun Kikuchi1,2,3, Takashi Nishihara1, Kazuo Shinozaki2,4 & Takashi

TOA 5:00 pm

TOA 5:30 pm

TOA 6:00 pm

TOA 6:15 pm

04:00-06:30 pm

TOB 4:00 pm

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Hirayama1,2,4, 1Grad. Sch. Integ. Sci., Yokohama City Univ; 2GSC, RIKEN Yokohama Inst.; 3CREST, JST & 4Plant Mol. Biol. Lab., RIKEN Tsukuba Inst. TOB 6:00 pm Restoration of hepatocyte function during decompression in human obstructive jaundice using 1H and 31P NMR spectroscopy of bile: Lakshmi Bala1, Pratima Tripathi1, G.A.Nagana Gowda1, C.L.Khetrapal1, Gunjan Shukla2 and Gourdas Choudhuri2, 1Centre of Biomedical Magnetic resonance and 2 Department of Gastroenterology Sanjay Gandhi Post Graduate Institute of Medical Sciences Raebareli Road, Lucknow- 226 014, India Tuesday afternoon parallel session C Nucleic Acid Structures-II, Hall C Chairpersons: S Butcher & B J Rao Protein and RNA dynamics play key roles in molecular recognition: Gabriele Varani, Zahra Shajani, Priti Deka and Gary Drobny,Department of Chemistry and Department of Biochemistry University of Washington, Seattle WA 98195-1700 USA Structure of hnRNP D Complexed with Telomere DNA, Unfolding of Quadruplex, and Discrimination of Intra- and Intermolecular Hydrogen Bonds: M. Katahira1, 1Yokohama National University, Yokohama, Japan Interaction of double-stranded RNA dependent protein kinase with HIV TAR RNA: Insil Kim, Corey Liu, and Joseph D. Puglisi, Stanford Magnetic Resonance Laboratory and Department of Structural Biology, Stanford University School of Medicine, Stanford, CA 94305-5126 Solution Structures of DNA Duplexes Containing Oxidative Cytosine Lesions: Varatharasa Thiviyanathan, Anoma Somasunderam, David E. Volk, Tapas K. Hazra, Sankar Mitra and David G. Gorenstein, Department of HBCG, University of Texas Medical Branch, Galveston, TX 77555, USA Hix DNA site that is out of contact with Hin protein adds specificity to the Hin-hix recognition: Sung-Hun Bae,1 Dawei Sun,1 Jongchul Bang,1 Jae-Sun Shin,1 Byong-Seok Choi,1,1Dept. of Chemistry, Korea Advanced Institute of Science and Technology, Republic of Korea RNA thermometers: Saheli Chowdhury (1,2), Christophe Maris (2), Frederic Allain (2) and Franz Narberhaus (1,3), (1) Institute of Microbiology, ETHZentrum, CH-8092 Zuerich, Switzerland; (2) Institute for Molecular Biology and Biophysics, ETH-Hönggerberg, CH-8093 Zuerich, Switzerland; (3) Lehrstuhl fuer Biologie der Mikroorganismen, Ruhr-Universitaet Bochum, D 44780 Bochum, Germany VISIT TO CRAFT VILLAGE, SHILPARAMAM Transfer to Indian Institute of Chemical Technology, Hyderabad for Dinner DINNER at Indian Institute of Chemical Technology, Hyderabad WEDNESDAY, January 19 9:00-10:30 am Wednesday morning PLENARY SESSION, Hall A

4:00-6:30 pm

TOC 4:00 pm

TOC 4:30 pm

TOC 5:00 pm

TOC 5:30 pm

TOC 5:45 pm

TOC 6:00 pm

6:15-7:15 pm 7:15 pm

8:00 pm

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Chairperson: Gil Navon Plenary 9:00 am Protein-RNA Recognition Events in RNA Interference: Dinshaw J. Patel, Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY, 10021, USA The SAIL Method for Protein NMR Spectroscopy: Masatsune Kainosho, CREST of JST and Graduate School of Science, Tokyo Metropolitan University BREAK (Tea and cookies), Shilpakala Vedika Lawns Wednesday morning parallel session A Protein Folding, Hall A Chairpersons: C M Dobson & Jayant Udgaonkar NMR Studies of the Protein Folding Landscape: H. Jane Dyson, Maria A. Martinez-Yamout and Peter E. Wright, Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla CA 92037. Protein Folding Dynamics studied by Spin Relaxation: Mikael Akke1, Kaare Teilum1, Patrik Lundstršm1, Frans A. A. Mulder1 and Flemming M. Poulsen2, 1 Department of Biophysical Chemistry, Lund University, Sweden, 2 Department of Protein Chemistry, University of Copenhagen, Denmark NMR in isotropic and anisotropic phase to monitor the folding of a stable native -hairpin via RDCs: Sebastian Meier and Stephan Grzesiek, Division of Structural Biology, Biozentrum der UniversitŠt Basel, 4056 Basel,Switzerland Structural characterization of the partially collapsed apo-form of a EFhand calcium binding protein and its folding to holo state: Sulakshana Mukherjee, Kavita Kuchroo, and Kandala V.R. Chary, Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400 005 India Residue-resolved structure, stability, folding and unfolding rates of kinetic protein folding intermediates measured by NMR: Mallela M. G. Krishna, Yan Lin, Leland Mayne & S. Walter Englander, Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, PA, USA 191046059 Residual structure and slow dynamics in α-synuclein: Carlos Bertoncini, Claudio O. Fernandez, Wolfgang Hoyer, Christian Griesinger, Thomas M. Jovin, Markus Zweckstetter,Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany Wednesday morning parallel session B Membrane Proteins, Hall B Chairpersons: R Norton & D Balasubramaniam Solution NMR Studies of Polytopic Helical Membrane Proteins in Micelles and Bicelles: Sebastien Poget, Douglas Kamen, Sean Cahill, and Mark Girvin, Biochemistry Department, Albert Einstein College of Medicine, 1300 Morris Park Ave, Bronx, NY 10461 Solution NMR Approaches for the Determination of High-Resolution Structures of Integral Membrane Proteins: J. Bushweller1, T. Cierpicki1, Y.

Plenary 9:45 am 10:30-11:00 am 11:00-1:00 pm

WOA 11:00 am

WOA 11:30 am

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WOA 12:30 pm

WOA 12:45 pm

11:00-1:00 pm

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Zhou1, B. Liang1, L. Tamm1, 1Molecular Physiology and Biological Physics, University of Virginia, Virginia, USA WOB 12:00 pm Membrane Protein in the remodelling shop: new properties for an old problem: Konstantin V. Pervushin, Laboratory of Physical Chemistry ETH Honggerberg, HCI F215 CH-8093 Zurich, Switzerland NMR Structural studies of nAChR M2 peptide: Yongae Kim1, Tae-Joon Park1, Mike Meslea2, and Stanley J. Opella2, 1: Dept. of Chemistry, HanKuk Univ. of Foreign Studies, YongIn, 449-791, KOREA, 2: Dept. of Chem. & Biochem., Univ. of Cal. San Diego, LaJolla, 92093-0307, USA Consequences of Acylation on Electrostatic Potential Distribution and Membrane Binding Properties of Dermaseptin Derivative K 4-S4(1-13) : Deborah E. Shalev1, Shahar Rotem2 and Amram Mor2, 1The Wolfson Centre for Applied Structural Biology, Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, 91904 Jerusalem, Israel, 2Department of Biotechnology & Food Engineering, Technion - Israel Institute of Technology, 32000 Haifa, Israel Wednesday morning parallel session C Imaging-II, Hall C Chairpersons: R A Kamoroski & S K Sarkar Functional Imaging of Cancer: Zaver M. Bhujwalla, JHU ICMIC Program, Department of Radiology, The Johns Hopkins University School of Medicine, Baltimore, MD 21205 Magnetic resonance in the developing brain: DG Gadian, Institute of Child Health, University College London, UK High resolution in vivo MRI and MRS of murine models of human neuropathologies: Patrick J. Cozzone and Angele Viola, Centre de Resonance Magnetique Biologique et Medicale (CRMBM) UMR CNRS 6612, Faculte de Medecine 27 Bd. Jean Moulin, 13005, Marseille (France) NEURAL MAPPING OF AUDITORY LEXICAL PROCESSING THROUGH FUNCTIONAL MRI: Y. Uma Sreekumar, S.S. Kumaran, S. Khushu and R.P. Tripathi, NMR Research Centre, Institute of Nuclear Medicine and Allied Sciences, Brig. S.K. Mazumdar Road, Delhi – 110 054, INDIA 3D Proton MR Spectroscopic Imaging of Prostate in Men with raised PSA: Virendra Kumar*, R. Kumar#, S.C Das #, S Thulkar@, S. Duttagupta$, A.K Hemal#, N.P Gupta# and N.R Jagannathan*, Departments of NMR*, Urology# and Pathology$ All India Institute of Medical Sciences, New Delhi – 110029. INDIA LUNCH BREAK Sampradaya Vedika Wednesday afternoon parallel session Methods-III, Hall A Chairpersons: Ad Bax & V S S Sastry Studies of protein dynamics and a new method to study drug/target interactions: Carlos Bertoncini, Min-Kyu Cho, Claudio Fernandez, Henrike Heise, Marcel Reese, Fernando Rodriguez-Castaneda, Victor Sanchez, Marc Baldus, Teresa Carlomagno, Tom Jovin, Markus Zweckstetter, Christian

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Griesinger, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen WOA 2:30 pm Collagen as a Chiral Agent, Revealed for the First Time by NMR: Gil Navon, Uzi Eliav, School of Chemistry, Tel Aviv University, Tel Aviv 69978, Israel Assignment of Side Chain Resonances of Uniformly 13C-labeled Large Proteins: Daiwen Yang1; Yu Zheng1; Chien Ho2;Yingqi Xu1, 1Department of Biological Sciences and Department of Chemistry, National University of Singapore,14 Science Drive 4, Singapore 117543, 2Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15213, USA G-Matrix Fourier Transform NMR Spectroscopy for Complete Protein Resonance Assignments: Hanudatta S. Atreya and Thomas Szyperski, Department of Chemistry and Structural Biology, State University of New YorkNortheast Structural Genomics Consortium, Buffalo, NY 14260 Probing Slow Backbone Dynamics in Proteins using TROSY-based Experiments to Detect Cross-correlated Time-modulation of Isotropic Chemical Shifts: Ranajeet Ghose*1,2 & Ananya Majumdar3, 1Department of Chemistry, City College of the City University of New York, New York, NY, 2 Graduate Programs in Chemistry and Biochemistry, Graduate Center of the City University of New York, New York, NY, 3Johns Hopkins University, Baltimore, MD Wednesday afternoon parallel session B ESR, Hall B Chairpersons: M C Krishna & B A Sastry Oxygen Physiology with In Vivo EPR Imaging: Howard J. Halpern,a,b ,Chad R. Haney,a,b Adrian Parasca,a,b Kazuhiro Ichikawa,a,b,e Eugene D. Barth,a,b Benjamin B. Williams, a,b Martyna Elas, a,b,c V.S. Subramanian,a,b Marta A. Zamora,d Jonathan N. River,d Gregory S. Karczmar,d Helena J. Mauceri,b Ralph R. Weichselbaum,b Colin Mailer,a,b Charles A. Pelizzari a,b , Gareth R. Eatonf, George A. Rinardf and Richard Quinef, aCenter for EPR Imaging In Vivo Physiology ,Departments ofb Radiation Oncology, University of Chicago, Chicago IL 60637 ,dRadiology, University of Chicago, Chicago IL 60637, e Biophysics, Kyushu University, Fukuoka, JP, c Molecular Biology, Jagiellonian University, Cracow, PO Applications of Hyperpolarized 13C and 15N: Klaes Golman EPR Spin Label Studies on Biological Cells and Membranes: Potential and Prospects for Radiobiological Research: K.P. Mishra., Bhabha Atomic Research Centre Radiation Biology and Health Sciences Division, Mumbai 400 085 The Large-Internal-Cavities of Fe and Mn Lipoxygenases: Betty J. Gaffney. Ann N. Imber. Fayi Wu. and Gurunathan Laxmikanthan. * Departments of Biological Sciences and *Chemistry and Biochemistry Florida State University. Tallahassee FL 32306 ESR-Investigation of The System On The Base Of Microcrystalline Cellulose and Drug substances: S.A.Muratova,1N.D.Burkhanova,1 G.V.Nikonovich1, S.Rashidova1, Institute of Polymer Chemistry and Physics,

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Academy of Sciences, Republic of Uzbekistan, 7b, A.Kadyrii S tr.,700 128, Tashkent 2:00-4:00 pm Wednesday afternoon parallel session C Oligosaccharides and Proteins, Hall C Chairpersons: G Valensin & K N Ganesh NMR Structure Determination of Bacterial Secondary Cell Wall Polymer Oligosaccharides: N. Müller,1 L. Trantirek,1 C. Steindl,1 C. Schäffer,2 P. Messner2, 1Johannes Kepler University, Linz, Austria, 2University of Natural Resources and Applied Life Sciences, Vienna, Austria Application of stable-isotope-labeling of glycopeptides to NMR analyses of sugar recognition by the intracellular lectins that determine the fates of glycoproteins in cells: Yoshiki Yamaguchi,1,2 Takeshi Hirao,1,2 Yukiko Kamiya,1,2 Noriko Takahashi,1,2 Koichi Kato1,2,3,4, 1Nagoya City University, Nagoya, Japan, 2CREST/JST, Saitama, Japan, 3RIKEN/GSC, Yokohama, Japan, 4 Institute for Molecular Science, Okazaki, Japan De Novo Design and Characterization of Glycosaminoglycan Binding Oligopeptides: G Jayaraman# and PC Lyu, Department of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan Structural Investigation of the Human Hepatic Asialoglycoprotein Receptor and some D-Galactose Complexes: A.M. Bianucci^, F. Chiellini°, A.M. Piras°, K. H. Mayo*, L. J. Yao#, M. Spiess&, ^Department of Pharmaceutical Science – University of Pisa, Italy, °Department of Chemistry & Industrial Chemistry – University of Pisa, Italy, *Department of Biochemistry, Molecular Biology & Biophysic – University of Minnesota, Minneapolis, USA., #Department of Chemistry – University of Minnesota, Minneapolis, USA, &Department of Biochemistry Biozentrum – University of Basel, Basel (Switzerland) Towards Understanding the Conformation and Dynamics of Biologically Important Oligosaccharide Systems: C. Baby 1, M.S. Moni 1 and S. Subramanian 2, 1Sophisticated Analytical Instrumentation Facility, Indian Institute of Technology Madras, Chennai-600036, INDIA, 2Radiation Biology Branch, National Cancer Institute, NIH, Bethesda, MD 20892, USA Stathmin-Like Domain N-Terminal Peptides Impede Tubulin Polymerization: M.J. Clement,1 I. Jourdain,2 S. Lachkar,2 P. Savarin, 2 A. Sobel,2 P.A. Curmi,1 F. Toma,1, 1 Universite Evry-Val d Essonne; Laboratoire Structure et Reconnaissance des Biomolecules, EA3637, Evry, France, 2 INSERM, U440, Institut du Fer a Moulin, Paris, France; UPMC, Paris, France Helix insertion to eject a ligand: a global conformational transition in the pheromone-binding protein of Bombyx mori: Fred F. Damberger1, Erich Michel1, Reto Horst1, Donghan Lee1, Walter S. Leal2, Kurt Wüthrich1,, 1Institut für Molekularbiologie und Biophysik, Eidgenössische Technische HochschuleZürich, CH-8093 Zürich, Switzerland, 2Department of Entomology, University of California, Davis, CA 95616, USA BREAK (tea and cookies), Shilpakala Vedika Lawns Wednesday afternoon ICMRBS –Founder’s Medal Presentation & Winners Lecture, Hall A Chairperson: R Kaptein

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Model Free formalism for NMR relaxation analysis: How far can we go?: S.-L. Chang1, A. Szabo2 & N. Tjandra1, 1Laboratory of Biophysical Chemistry, NHLBI, 2Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, MD 20892, U. S. A. 5:45 pm EXCURSION TO GOLKONDA FORT; Light and Sound show; with packed dinners THURSDAY, January 20 9:00-10:30 am Thursday morning PLENARY SESSION, Hall A Chairperson: H. Rueterjans Metalloproteins and advancements in NMR: Ivano Bertini, CERM, Via L. Sacconi 6, Sesto Fiorentino 50019, ITALY Time-Domain Radiofrequency EPR for in Vivo Imaging Applications: Murali C. Krishna, Nallathamy Devasahayam, Ramachandran Murugesan, KenIchiro Matsumoto, Sankaran Subramanian, James B.Mitchell, Radiation Biology Branch, Center for Cancer Research, National Cancer Institute NIH, Bethesda, Maryland, USA BREAK (Tea and cookies), Shilpakala Vedika Lawns Thursday morning parallel session A Methods-IV, Hall A Chairpersons R A Byrd & S Roy NMR Approach for the Structural Determination of Protein Interfaces in Complexes: Fabien Ferrage, Alex Shekhtman, Kaushik Dutta, Rong Xu, David Cowburn, New York Structural Biology Center, New York, New York High level cell-free expression and specific labelling of integral membrane proteins: F. Bernhard1, C. Klammt1, V. Dötsch1, 1Johann Wolfgang GoetheUniversity, Frankfurt/Main, Germany Enzyme Function by Solid State NMR: Cytochrome P450: Ann E McDermott1, Tijana Jovanovic1, Micheal Harris1, 1Columbia University, New York, NY USA.

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High Expression with Corynebacterium glutamicum for NMR Sample Preparation: M. Shinagawa,1 N. Shimba,1 T. Mizukoshi,1 N. Yamada,1 Y. Kikuchi,1 and E. Suzuki.1, 1Ajinomoto Co., Japan Cell free translation methods for NMR use: M Neerathilingam1, L.H.Greene2, S.A.Colebrooke1, D Staunton1 and I.D. Campbell 1, 1Department of Biochemistry, University of Oxford, Southparks Road,Oxford,OX1 3QU 2 University College London, Department of Biochemistry, Darwin Building, Gower Street, London,WC1E 6BT The hetero-nuclear NMR-based metabolomics reveals incorporation of and 15N-compounds into higher plants: Kenji Akamine1, Takashi Hirayama1,2,3 Jun Kikuchi1,2,4, 1Grad. Sch. Integ. Sci., Yokohama City Univ,
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GSC, RIKEN Yokohama Inst, 3Plant Mol. Biol. Lab., RIKEN Tsukuba Inst, CREST, JST

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Thursday morning parallel session B Computational Methods, Hall B Chairpersons: M Garland & Anil Saran Extraction of information from NMR spectra: M. Billeter,1 D. Malmodin,1 T. Luan 2, 1 Biophysics Group, Department of Chemistry, Göteborg University, Sweden, 2 Swedish NMR Centre, Göteborg University, Sweden Automated NMR Structure Calculation with Cyana: Peter Güntert, Tatsuo Miyazawa Memorial Program, RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama 230-0045, Japan ISD, a probabilistic principle for structure determination by NMR: M. Habeck,1 W. Rieping,1 M. Nilges,1, 1Structural Bioinformatics Unit, CNRS URA 2185, Pasteur Institute, 25-28 rue du docteur Roux, F-75015 Paris, France Shedding Light on the Rhodopsin/Transducin Interface: L. Q. Anderson1, M. A. Anderson1, N.Van Eps2, S. O. Smith3, W. L. Hubbell2, T. J. Baranski1, O. G. Kisselev4, G. R. Marshall1, 1Washington University, Missouri; 2UCLA, California; 2SUNY Stony Brook, New York; 4St. Louis University, Missouri, USA Automated Structure Improvement and Verification of Proteins from NMR and X-ray data: W. Gronwald, J. Trenner, K. Brunner, B. Ganslmeier, A. Nassar, R. Kirchhöfer, K.-P. Neidig and H. R. Kalbitzer, Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93040 Regensburg, Germany and Bruker Biospin, 76287Rheinstetten, Germany Probing weakly structured conformational ensembles with residual dipolar couplings: M. Louhivuori,1 K. Fredriksson,2 A. Annila,1,3, 1Department of Physical Sciences, 2Program in Structural Biology and Biophysics Program, Institute of Biotechnology, and 3Department of Biosciences, University of Helsinki, Finland Thursday morning parallel session C Membrane Proteins-II, Hall C Chairpersons: A G Redfield & S R Kasturi Field-Cycling NMR in a Shared Commercial Spectrometer: Applications to Nucleic Acids, Proteins, and especially Membranes (and lots more!): A.G. Redfield, Brandeis, University, and Mary F. Roberts, Boston College. Membrane Interactions of the Pore-forming Protein Equinatoxin II: 19F NMR Studies: R.S. Norton,1 G. Anderluh,2 A. Razpotnik,2 Z. Podlesek,2 F. Separovic3, 1 Walter and Eliza Hall Institute of Medical Research, Parkville 3050, Australia, 2 Department of Biology, Biotechnical Faculty, University of Ljubljana, 1000 Ljubljana, Slovenia, 3 School of Chemistry, University of Melbourne, 3010, Australia NMR Strategy for Membrane Proteins-ligands Interactions: Ichio Shimada1,2, Graduate School of Pharmaceutical Sciences, the University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

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Solid-State Deuterium NMR Spectroscopy of Retinal Proteins in Aligned Membranes: Michael F. Brown,1,2 Gilmar F. J. Salgado,3 Andrey V. Struts,1 Katsunori Tanaka,4 Naoko Fujioka,4 Sonja Krane,4 Koji Nakanishi4, Departments of 1Chemistry, 2Physics, and 3Biochemistry & Molecular Biophysics, University of Arizona, Tucson, Arizona 85721, USA, 4Department of Chemistry, Columbia University, New York, New York 10027, USA LUNCH BREAK Sampradaya Vedika POSTER SESSION and EXHIBITS, Halls D &E (with tea and cookies) Even numbered posters are discussed during this time. Transfer to hotels to refresh on their way to Ramoji Film city for Banquet Dinner Pick-up from hotels for Banquet Dinner DINNER Ramoji Film City, Hyderabad FRIDAY, January 21

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Friday morning parallel session A Proteins-II, Hall A Chairpersons D Cowburn & S Cowsik Auto-inhibition Mechanism of X11s/Mints Family Scaffold Proteins Revealed by the Closed Conformation of the Tandem PDZ Domains: Jia-Fu Long, Wei Feng, Ling-Nga Chan, Mingjie Zhang, Department of Biochemistry, Molecular Neuroscience Center, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, P. R. China Domain motion in cytochrome P450 reductase studied by domain-specific isotope labeling: Jackie Ellis1, Igor L. Barsukov1 and Gordon C.K. Roberts1, 1 Biological NMR Centre, Department of Biochemistry, University of Leicester, PO Box 138, Leicester LE1 9HN, United Kingdom NMR studies on structure and dynamics in transcription and translation: Rolf Boelens, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands How structure and stability influence the function of tea domain transcription factors: Asokan Anbanandam and Sudha Veeraraghavan, Department of Biochemistry and Molecular Biology and Structural Biology Research Center, UT-Houston Medical School, Houston, TX 77030 Structure and dynamics in solution of the complex of human dihydrofolate reductase with trimethoprim and NADPH: Nadezhda V. Kovalevskaya1, Vladimir I. Polshakov1,2, Berry Birdsall3, Alan F. Bradbury3, Thomas A. Frienkel4 and James Feeney3, 1 Center for Drug Chemistry, Moscow, Russia, 2 Research Center for Magnetic Tomography & Resonance, M.V. Lomonosov Moscow State University, Moscow, Russia, 3 National Institute for Medical Research, London, United Kingdom, 4 MRC Biomedical NMR Center, London, United Kingdom Folding Regulates Auto-processing of HIV-1 Protease Precursor: Amarnath Chatterjee1, Mridula P.1, Ram Kumar Mishra2, Rohit Mittal2, R. V. Hosur1,

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Dept. of Chemical Sciences, 2Dept. of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba Mumbai- 400005, India 9:00-11:15 am Friday morning parallel session B SS NMR-II, Hall B Chairpersons: T Fujiwara & K V Ramanathan Structure Determination of Coat Proteins in Virus Particles: Stanley J. Opella, Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92037-0307 USA Structural studies of large membrane embedded proteins in natural membranes using solid state NMR: Anthony Watts, Department of Biochemistry, University of Oxford, Oxford, UK High Frequency Dynamic Nuclear Polarization: R.G. Griffin, Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139 Structure studies of protein complexes with solid-state magic-angle spinning NMR: B.-J. van Rossum,1 L. Krabben,1 M. Hiller,1 F. Castellani,1 A. Diehl,1 K. Rehbein,1 C. Weise,2 F. Hucho,2 E. Bocharov,3 A. A. Shuga,3 A. Arseniev3, V. Kumar,4 W. Kühlbrandt4 and H. Oschkinat1, 1Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany, 2Institut für Biochemie, Freie Universität Berlin, Germany, 3Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia, 4MPI of Biophysics, Frankfurt/Main, Germany Dependence of protein solid state NMR spectra on the crystal environment: Hans Jürgen Sass & Stephan Grzesiek, Division of Structural Biology, Biozentrum der Universität Basel, Klingelbergstr. 70, CH-4056 Basel, Switzerland Heteronuclear Scalar Correlation between Carbon and DQ Proton Chemical shifts in Solids: Vipin Agarwal (a), K.V.Ramanathan (a), Anne Lesage (b) and Lyndon Emsley (b), (a) Sophisticated Instrument Facility, Indian Institute of Science, Bangalore, India, (b) Laboratoire de Chimie, UMR-5182 CNRS/ENS, Ecole Normale Superieure de Lyon, France. Friday morning parallel session C Drug Design, Hall C Chairpersons: M Ikura & S Pentyala Structure-activity studies on circular proteins: David J Craik, Norelle L Daly, Fiona M Foley, Lillian Sando and Shane Simonsen, Institute for Molecular Bioscience, University of Queensland, Brisbane 4072, Australia NMR investigations of Kinases and Phosphatases: Harald Schwalbe, Center for Biomolecular Magnetic Resonance, Institute for Organic Chemistry and Chemical Biology, Marie-Curie-Str. 11, 60439 Frankfurt/Main, Germany Development of small molecule inhibitors of S100B: David J. Weber and Joseph Markowitz, University of Maryland, School of Medicine

1

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Solution NMR structural studies of consus peptides from Indian marine snails: Siddhartha P. Sarma1*, Sujit K. Sikdar1, K.S.Krishnan2 and P.Balaram1, Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India, Department of Biological Sciences, Tata Institute of Fundamental Research, Mumbai 400 005, India Conformational study of cyclic peptides containing exclusive cis Xaa-Pro amide bond derived via ring closing metathesis: S. Kiran Kumar,a B. M. Rajesh,b K. Vyas,b J. Moses Babu,b R. Vasudev,b Javed Iqbalb and A. C. Kunwar.a, Centre for Nuclear Magnetic Resonance, Indian Institute of Chemical Technology, Hyderabad-500 007, India. (b) Discovery Research, Dr. Reddy’s Research Foundation, Bollaram road, Miyapur, Hyderabad-500 050, India Nucleation of -Hairpin Structures by a Three Residue Turn in a Designed Synthetic Nonapeptide: S. Raghothama1, Rajkishor Rai 2and P. Balaram2, 1 Sophisticated Instruments Facility and 2Molecular Biophysics Unit, Indian Institute of Science, Bangalore – 560 012. India BREAK (Tea and cookies), Shilpakala Vedika Lawns Friday morning plenary session & concluding remarks Hall A Chairpersons: S J Opella & C L Khetrapal

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Weak Alignment Provides Unique Opportunities in NMR Studies of Biomolecules: David Bryce, Chris Jaroniec, Jerome Boisbouvier, Emeric Miclet,Erin OÕNeil-Cabello, Tobias Ulmer, Justin Wu, Alex Grishaev, and Ad Bax, Laboratory of Chemical Physics, NIDDK, NIH, Bethesda, MD 20892, USA CONCLUDING REMARKS by Mastasune Kainosho FAREWELL LUNCH, Sampradaya Vedika

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ORAL + POSTER ABSTRACT PO 1 In-Cell NMR studies of various proteins expressed in E. coli: Masatoshi Yoshimasu1,2, Tsutomu Mikawa2,3,4, Nobuhiro Hayashi5, Takehiko Shibata1,3,4, and Yutaka Ito2,3,4, 1Cellular and Molecular Biology Laboratory and 3Research Group of Bio-supramolecular Structure-Function, RIKEN, JAPAN; 2CREST/JST; 4Graduate School of Integrated Science, Yokohama-City University, JAPAN; 5Fujita Health University, JAPAN. Novel Probes for Magnetic Resonance Imaging: A.Manivannan1 and S. Sendhil Velan2, 1 Physics Department, 2Center for Advanced imaging and Radiology, West Virginia University,Morgantown, WV 26506, USA Alignment tensor determination for a weakly-aligned protein based on orientation-induced TROSY chemical shift changes: Shin-ichi Tate1, and Hiroshi Moriuchi1, 1Biomolecular Engineering Research Institute (BERI), Osaka, Japan Sample Patterning on the Surface of Planar NMR-Microcoils: K. Ehrmann1, M. Gersbach1, P. Pascoal2, F. Vincent1, C. Massin1, D. Stamou2, P.-A. Besse1, H. Vogel2 and R.S. Popovic1, 1 Institute of Microsystems, 2Institute of Chemical Sciences, EPFL – Swiss Federal Institute of Technology Lausanne, CH-1015 Lausanne, Switzerland G-Matrix Fourier Transform NMR Spectroscopy for Complete Protein Resonance Assignments: Hanudatta S. Atreya and Thomas Szyperski, Department of Chemistry and Structural Biology, State University of New York, and Northeast Structural Genomics Consortium, Buffalo, NY 14260 Probing Slow Backbone Dynamics in Proteins using TROSY-based Experiments to Detect Cross-correlated Time-modulation of Isotropic Chemical Shifts: Ranajeet Ghose*1,2 & Ananya Majumdar3, 1Department of Chemistry, City College of the City University of New York, New York, NY,2Graduate Programs in Chemistry and Biochemistry, Graduate Center of the City University of New York, New York, NY, 3Johns Hopkins University, Baltimore, MD High Expression with Corynebacterium glutamicum for NMR Sample Preparation: M. Shinagawa,1 N. Shimba,1 T. Mizukoshi,1 N. Yamada,1 Y. Kikuchi,1 and E. Suzuki.1, 1Ajinomoto Co., Japan. Cell free translation methods for NMR use: M Neerathilingam1, L.H.Greene2, S.A.Colebrooke1, D Staunton1 and I.D. Campbell1, 1Department of Biochemistry, University of Oxford, Southparks Road,Oxford,OX1 3QU. 2University College London, Department of Biochemistry, Darwin Building, Gower Street, London,WC1E 6BT The hetero-nuclear NMR-based metabolomics reveals incorporation of 13C and 15Ncompounds into higher plants: Kenji Akamine1, Takashi Hirayama1,2,3 ,Jun Kikuchi1,2,4, 1Grad. Sch. Integ. Sci., Yokohama City Univ; 2GSC, RIKEN Yokohama Inst.; 3Plant Mol. Biol. Lab., RIKEN Tsukuba Inst. And 4CREST, JST Investigation of uniformly 13C/15N labeled alpha-Synuclein Fibrils with Multidimensional MAS Solid-State NMR: H. Heise, W. Hoyer, S. Becker, V. Subramaniam, T.M. Jovin, M. Baldus, Max-Planck-Institut für Biophysikalische Chemie, Am Fassberg 11, 37077 Göttingen, Germany

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Novel Solid-State NMR Approach to Structural Analysis of Proteins: Application to Phoborhodopsin Transducer pHtrII in Lipid Membrane Environment: Yoh Matsuki1,4, Yuki Sudo2, Chojiro Kojima3, Toshimichi Fujiwara4, Naoki Kamo2, Hideo Akutsu4,1JSTBIRD,2Graduate School of Pharmaceutical Science, Hokkaido University, 3Graduate School of Biological Science, Nara Institute for Science and Technology, 4Institute for Protein Research, Osaka University Phase modulated Lee-Goldberg sequence and proton spectroscopy in solid-state: P. K. Madhu, Elena Vinogradov, Leon Bosman, and Shimon Vega, Department of Chemical Sciences, Tata Institute of Fundamental Research, Colaba, Mumbai 400 005, India, Department of Chemical Physics, Weizmann Institute of Science, Rehovot 76100, Israel Structure studies of protein complexes with solid-state magic-angle spinning NMR: B.-J. van Rossum1, L. Krabben1, M. Hiller1, F. Castellani1, A. Diehl1, K. Rehbein1, C. Weise2, F. Hucho2,E. Bocharov3, A. A. Shuga3, A. Arseniev3, V. Kumar4, W. Kühlbrandt4 and H. Oschkinat1, 1 Forschungsinstitut für Molekulare Pharmakologie, Berlin, Germany, 2Institut für Biochemie, Freie Universität Berlin, Germany, 3Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia, 4MPI of Biophysics, Frankfurt/Main, Germany Dependence of protein solid state NMR spectra on the crystal environment: Hans Jürgen Sass & Stephan Grzesiek, Division of Structural Biology, Biozentrum der Universität Basel, Klingelbergstr. 70, CH-4056 Basel, Switzerland Heteronuclear Scalar Correlation between Carbon and DQ Proton Chemical shifts in Solids: Vipin Agarwal1, K.V.Ramanathan1, Anne Lesage2 and Lyndon Emsley2, 1Sophisticated Instrument Facility, Indian Institute of Science, Bangalore, India, 2Laboratoire de Chimie, UMR5182 CNRS/ENS, Ecole Normale Superieure de Lyon, France Structural Proteomics of Eukaryotic Protein Domain Families: G. V. T. Swapna, Gaetano T. Montelione and the Northeast Structural Genomics Consortium, Center for Advanced Biotechnology Medicine, Rutgers University, Piscataway, NJ 08854 Monitoring NMR Protein Structure Quality by Molecular Replacement: Michael A. Kennedy, Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA, 99354 How Structure and Stability influence the function of TEA domain Transcription Factors: Asokan Anbanandam and Sudha Veeraraghavan, Department of Biochemistry and Molecular Biology and Structural Biology Research Center, UT-Houston Medical School, Houston, TX 77030 Structure and dynamics in solution of the complex of human dihydrofolate reductase with trimethoprim and NADPH: Nadezhda V. Kovalevskaya1, Vladimir I. Polshakov1,2, Berry Birdsall3, Alan F. Bradbury3, Thomas A. Frienkel4 and James Feeney3, 1 Center for Drug Chemistry, Moscow, Russia, 2 Research Center for Magnetic Tomography & Resonance, M.V. Lomonosov Moscow State University, Moscow, Russia, 3 National Institute for Medical Research, London, United Kingdom, 4 MRC Biomedical NMR Center, London, United Kingdom Folding Regulates Auto-processing of HIV-1 Protease Precursor: Amarnath Chatterjee1, Mridula P.1, Ram Kumar Mishra2, Rohit Mittal2, R. V. Hosur1, 1Dept. of Chemical Sciences, 2 Dept. of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai- 400005, India Alternative Conformations of the gp120 V3 Loop suggest a mechanism for HIV-1 coreceptor selectivity and the Molecular Basis for Broad Neutralization by antibody 447-52D: Osnat Rosen, Michal Sharon and Jacob Anglister, Department of Structural Biology, The Weizmann Institute of Science, Rehovot 76100, Israel.

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Folding Mechanism of SUMO-1: Non Native Structural characteristics of equilibrium intermediates: Ashutosh Kumar1, Sudha Srivastva1, Ram Kumar Mishra2, Rohit Mittal2, Ramkrishna V. Hosur1, 1Dept. of Chemical Sciences, 2Dept. of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai- 400005, India NMR in isotropic and anisotropic phase to monitor the folding of a stable native -hairpin via RDCs: Sebastian Meier and Stephan Grzesiek, Division of Structural Biology, Biozentrum der Universit·t Basel, 4056 Basel, Switzerland Structural characterization of the partially collapsed apo-form of a EF-hand calcium binding protein and its folding to holo state: Sulakshana Mukherjee, Kavita Kuchroo, and Kandala V.R. Chary, Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400 005 India Residue-resolved structure, stability, folding and unfolding rates of kinetic protein folding intermediates measured by NMR: Mallela M. G. Krishna, Yan Lin, Leland Mayne & S. Walter Englander, Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia, PA, USA 19104-6059 Residual structure and slow dynamics in - synuclein: Carlos Bertoncini, Claudio O. Fernandez, Wolfgang Hoyer, Christian Griesinger, Thomas M. Jovin, Markus Zweckstetter, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany NMR studies of copper (II) interacting with peptides derived from the prion and the amyloid precursor proteins: Elena Gaggelli, Daniela Valensin and Gianni Valensin, Department of Chemistry, University of Siena, Via Aldo Moro, Siena 53100, Italy Roles of Noncoordinated Aromatic Residues in Redox Regulation of Cytochrome c3 from Desulfovibrio vulgaris Miyazaki F: Yuki Takayama1, Erisa Harada12, Rie Kobayashi3, Kiyoshi Ozawa3, and Hideo Akutsu1, Institute for Protein Research, Osaka University, Yamadaoka, Suita 565-0871, Japan, Japan 2Biological Informatics Consortium, Chuo-ku, Tokyo 104-0032, Japan, and Faculty of Engineering, 3Yokohama National University, Hodogaya-ku, Yokohama 240-8501, Japan Structural basis for the observed magnetic anisotropic tensorial values in a calcium binding protein: Sourajit M. Mustafi, Sulakshana Mukherjee and Kandala V.R Chary, Department of Chemical Sciences, Tata Institute of Fundamental Research, Mumbai, India NMR Structural studies of nAChR M2 peptide: Yongae Kim1, Tae-Joon Park1, Mike Meslea2, and Stanley J. Opella2, 1 Dept. of Chemistry, HanKuk Univ. of Foreign Studies, YongIn, 449-791, KOREA, 2Dept. of Chem. & Biochem., Univ. of Cal. San Diego, LaJolla, 92093-0307, USA Consequences of Acylation on Electrostatic Potential Distribution and Membrane Binding Properties of Dermaseptin Derivative K4-S4(1-13): Deborah E. Shalev1, Shahar Rotem2 and Amram Mor2, 1The Wolfson Centre for Applied Structural Biology, Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Safra Campus, Givat Ram, 91904 Jerusalem, Israel, 2Department of Biotechnology & Food Engineering, Technion - Israel Institute of Technology, 32000 Haifa, Israel Unusual Primer-Template Structures for Low-Fidelity DNA Polymerases: S. L. Lam and L. M. Chi, Department of Chemistry, The Chinese University of Hong Kong, Hong Kong Structure of daunomycin complexed with d-TGATCA by nuclear mangentic resonance spectroscopy and restrained molecular dynamics: Monica1, S.K.Barthwal2, R. Barthwal1, 1 Department of Biotechnology and 2Physics, Indian Institute of Technology Roorkee, 247667 India

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TRNOE analysis of the single-stranded DNA structure induced by binding of the yeast mitochondrial DNA recombination protein Mhr1p: Tokiha Masuda12, Tsutomu Mikawa12,3,4, Masatoshi Yoshimasu3,4, Feng Ling3, Takehiko Shibata1,2,3 and Yutaka Ito1,2,3,4, 1Molecular and Cellular Physiology Laboratory, Graduate School of Integrated Science, Yokohama City University, Japan; 2Research Group for Bio-supramolecular Structure-Function, RIKEN, Japan; 3 Cellular and Molecular Biology Laboratory, RIKEN, Japan; 4CREST/JST Solution Structures of DNA Duplexes Containing Oxidative Cytosine Lesions: Varatharasa Thiviyanathan, Anoma Somasunderam, David E. Volk, Tapas K. Hazra, Sankar Mitra and David G. Gorenstein, Department of HBCG, University of Texas Medical Branch, Galveston, TX 77555, USA Hix DNA site that is out of contact with Hin protein adds specificity to the Hin-hix recognition: Sung-Hun Bae1, Dawei Sun1, Jongchul Bang1, Jae-Sun Shin1, Byong-Seok Choi1, 1 Dept. of Chemistry, Korea Advanced Institute of Science and Technology, Republic of Korea. RNA thermometers: Saheli Chowdhury 1,2, Christophe Maris 2, Frederic Allain 2 and Franz Narberhaus 1,3, 1Institute of Microbiology, ETH-Zentrum, CH-8092 Zuerich, Switzerland; 2Institute for Molecular Biology and Biophysics, ETH-Hönggerberg, CH-8093 Zuerich, Switzerland; 3 Lehrstuhl fuer Biologie der Mikroorganismen, Ruhr-Universitaet Bochum, D-44780 Bochum, Germany Application of stable-isotope-labeling of glycopeptides to NMR analyses of sugar recognition by the intracellular lectins that determine the fates of glycoproteins in cells: Yoshiki Yamaguchi1,2, Takeshi Hirao1,2, Yukiko Kamiya1,2, Noriko Takahashi1,2, Koichi Kato1,2,3,4, 1 Nagoya City University, Nagoya, Japan, 2CREST/JST, Saitama, Japan, 3RIKEN/GSC, Yokohama, Japan, 4Institute for Molecular Science, Okazaki, Japan De Novo Design and Characterization of Glycosaminoglycan Binding Oligopeptides: G Jayaraman# and PC Lyu, Department of Life Sciences, National Tsing Hua University, Hsinchu, Taiwan. Structural Investigation of The Human Hepatic Asialoglycoprotein Receptor and some DGalactose Complexes: A.M. Bianucci^, F. Chiellini°, A.M. Piras°, K. H. Mayo*, L. J. Yao#, M. Spiess&, ^Department of Pharmaceutical Science – University of Pisa, Italy, °Department of Chemistry & Industrial Chemistry – University of Pisa, Italy, *Department of Biochemistry, Molecular Biology & Biophysic – University of Minnesota, Minneapolis, USA, #Department of Chemistry – University of Minnesota, Minneapolis, USA, &Department of Biochemistry Biozentrum – University of Basel, Basel (Switzerland) Towards Understanding the Conformation and Dynamics of Biologically Important Oligosaccharide Systems: C. Baby 1, M.S. Mon 1 and S. Subramaniam 2, 1 Sophisticated Analytical Instrumentation Facility, Indian Institute of Technology Madras, Chennai-600036, INDIA, 2Radiation Biology Branch, National Cancer Institute, NIH, Bethesda, MD 20892, USA. Stathmin-Like Domain N-Terminal Peptides Impede Tubulin Polymerization: M.J. Clement1, I. Jourdain2, S. Lachkar2, P. Savarin2, A. Sobel2, P.A. Curmi1, F. Toma1, 1 Universite Evry-Val d Essonne; Laboratoire Structure et Reconnaissance des Biomolecules, EA3637, Evry, France , 2 INSERM, U440, Institut du Fer a Moulin, Paris, France; UPMC, Paris, France Helix insertion to eject a ligand: a global conformational transition in the pheromonebinding protein of Bombyx mori: Fred F. Damberger1, Erich Michel1, Reto Horst1, Donghan Lee1, Walter S. Leal2, Kurt Wüthrich1, 1Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule-Zürich, CH-8093 Zürich, Switzerland, 2Department of Entomology, University of California, Davis, CA 95616, USA Solution structure of the UBA domain of budding yeast DSK2p in complex with the ubiquitin: Ayako Ohno1,2, JunGoo Jee2,3, Kenichiro Fujiwara2, Takeshi Tenno2,4, Natsuko Goda2,

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Hidehito Tochio2, Hideki Kobayashi5, Hidekazu Hiroaki1,2 Masahiro Shirakawa2,3, 1Kihara Memorial Yokohama Foundation for the advancement of Life Sciences, Kanagawa, Japan, 2 Yokohama City University, Kanagawa, Japan, 3RIKEN GSC, Kanagawa, Japan, 4Ehime University, Ehime, Japan, 5Kyushu University, Fukuoka, Japan PO45 Applications of NMR Spectroscopy and Structural Enzymology to Target-based Discovery of Novel Antibacterials: Gunther Kern, Per-Olof Eriksson, Tomas Lundqvist, Sushmita Lahiri, Elaina Zverina, Thomas A. Keating, Brian Noonan and Gautam Sanyal*, Infection Discovery, AstraZeneca R&D Boston, 35 Gatehouse Drive, Waltham, MA 02451, USA and Structural Chemistry Laboratory, AstraZeneca R&D Mölndal, Sweden Discovery of leads for the macrophage migration inhibitory factor using fragment-based screening. A synergistic application of NMR, MS and X-ray screening: C. Fernández, M.J.J. Blommers, F. Bitsch, A. Widmer, A. Marzinzik, S. Lehmann, J.-M. Rondeau, Novartis Institutes for Biomedical Research, Basel, Switzeland Solution NMR structural studies of conus peptides from Indian marine snails: Siddhartha P. Sarma1*, Sujit K. Sikdar1, K.S.Krishnan2 and P.Balaram1, 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560 012, India, 2Department of Biological Sciences, Tata Institute of Fundamental Research, Mumbai 400 005, India Conformational study of cyclic peptides containing exclusive cis Xaa-Pro amide bond derived via ring closing metathesis: S. Kiran Kumar1, B. M. Rajesh2, K. Vyas2, J. Moses Babu2, R. Vasudev2, Javed Iqbal2 and A. C. Kunwar1, 1Centre for Nuclear Magnetic Resonance, Indian Institute of Chemical Technology, Hyderabad-500 007, India, 2Discovery Research, Dr. Reddy’s Research Foundation, Bollaram road, Miyapur, Hyderabad-500 050, India Nucleation of  -Hairpin Structures by a Three Residue Turn in a Designed Synthetic Nonapeptide: S. Raghothama1, Rajkishor Rai2 and P. Balaram2, 1Sophisticated Instruments Facility and 2Molecular Biophysics Unit, Indian Institute of Science, Bangalore – 560 012, India 3D Proton MR Spectroscopic Imaging of Prostate in Men with raised PSA: Virendra Kumar*, R. Kumar#, S.C Das #, S Thulkar@, S. Duttagupta$, A.K Hemal#, N.P Gupta# and N.R Jagannathan*, Departments of NMR*, Urology# and Pathology$ All India Institute of Medical Sciences, New Delhi – 110029. INDIA NEURAL MAPPING OF AUDITORY LEXICAL PROCESSING THROUGH FUNCTIONAL MRI: Y. Uma Sreekumar, S.S. Kumaran, S. Khushu and R.P. Tripathi, NMR Research Centre, Institute of Nuclear Medicine and Allied Sciences, Brig. S.K. Mazumdar Road, Delhi – 110 054, INDIA Investigation of Muscle Metabolism by Multi-Dimensional Localized Magnetic Resonance Spectroscopic Techniques at 3T: S. Sendhil Velan1, Susan Lemieux1, Raymond R. Raylman1, M. Albert Thomas2, 1Center for Advanced Imaging and Department of Radiology, West Virginia University, 2Department of Radiology, University of California, Los Angeles Activation of the Brain Center Associated with Visually Evoked Sexual Arousal: Functional MR Imaging: Gwang Woo Jeong, Heoung Keun Kang, Hyung Joong Kim, Hyeong Jung Kim, Jeong Jin Seo, Department of Radiology, Chonnam National University Medical School, Gwangju 501-190, Korea The Regulation of GABA Synthesis during Increased Brain Activity: Anant B. Patel1, Robin A. de Graaf1, Kevin L. Behar2, Department of 1Diagnostic Radiology and 2Psychiatry, Magnetic Resonance Research Center, Yale University School of Medicine, New Haven, CT 06520, USA

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The hetero-nuclear NMR-based metabol(n)omics of plant and animal systems: Jun Kikuchi1,2,3, Takashi Nishihara1, Kazuo Shinozaki2,4 & Takashi Hirayama1,2,4, 1Grad. Sch. Integ. Sci., Yokohama City Univ; 2GSC, RIKEN Yokohama Inst.; 3CREST, JST & 4Plant Mol. Biol. Lab., RIKEN Tsukuba Inst. Restoration of hepatocyte function during decompression in human obstructive jaundice using 1H and 31P NMR spectroscopy of bile: Lakshmi Bala1, PratimaTripathi1, G.A.Nagana Gowda1, C.L.Khetrapal1, Gunjan Shukla2 and Gourdas Choudhuri2, 1Centre of Biomedical Magnetic resonance and 2Department of Gastroenterology, Sanjay Gandhi Post Graduate Institute of Medical Sciences, Raebareli Road, Lucknow- 226 014, India ESR-Investigation of The System On The Base Of Microcrystalline Cellulose and Drug substances: S.A.Muratova, N.D.Burkhanova, G.V.Nikonovich, S.Sh.Rashidova, Institute of Polymer Chemistry and Physics, Academy of Sciences, Republic of Uzbekistan, 7b, A.Kadyrii S tr.,700 128, Tashkent Shedding Light on the Rhodopsin/Transducin Interface: L. Q. Anderson1, M. A. Anderson1, N.Van Eps2, S. O. Smith3, W. L. Hubbell2, T. J. Baranski1, O. G. Kisselev4, G. R. Marshall1, 1 Washington University, Missouri; 2UCLA, California; 2SUNY Stony Brook, New York; 4St. Louis University, Missouri, USA Automated Structure Improvement and Verification of Proteins from NMR and X-ray data: W. Gronwald, J. Trenner, K. Brunner, B. Ganslmeier, A. Nassar, R. Kirchhöfer, K.-P. Neidig and H. R. Kalbitzer, Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93040 Regensburg, Germany and Bruker Biospin, 76287Rheinstetten, Germany Probing weakly structured conformational ensembles with residual dipolar couplings: M. Louhivuori1, K. Fredriksson2, A. Annila1,3, 1Department of Physical Sciences, 2Program in Structural Biology and Biophysics Program, Institute of Biotechnology, and 3Department of Biosciences, University of Helsinki, Finland.

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POSTER ABSTRACTS Methods P1 Reducing Decoupler heating by an Order of Magnitude in Triple-resonance MAS NMR at 750 MHz: F.David Doty1, Jatin Kulkarni1, George Entzminger1, Siddarth Shevgoor1, Kranti P. Shevgoor1, Tony Bielecki2,and Christopher Turner2 1Doty Scientific, 700 Clemson Rd., Columbia, SC, 29229, USA, 2Francis Bitter Magnet Lab, MIT, 170 Albany Street, Cambridge, MA, 02139, USA Side Chain Assignments of Methyl-Containing Residues in a Uniformly 13C-labeled Hemoglobin: Yu Zheng1 and Daiwen Yang1, 1Department of Biological Sciences and Department of Chemistry, National University of Singapore,14 Science Drive 4 Singapore 117543 Sample Patterning on the Surface of Planar NMR-Microcoils: K. Ehrmann1, M. Gersbach1, P. Pascoal2, F. Vincent1, C. Massin1, D. Stamou2, P.-A. Besse1, H. Vogel2 and R.S. Popovic1, 1 Institute of Microsystems, 2Institute of Chemical Sciences, EPFL – Swiss Federal Institute of Technology Lausanne, CH-1015 Lausanne, Switzerland High b-value q-space analysis of bovine muscle ex vivo: loss of fiber orientation dependent diffusion: E. Gedat1, S. Mueller2, A. Stroh3, J. Wuerfel2, T. Tolxdorff1, 1Institute of Medical Informatics, 2Clinic and Polyclinic for Neurology, 3Institute of Radiology, 4Institute of Neuroimmunology, Charite University Medicine Berlin, Germany Determination of residual dipolar couplings of the alpha carbon site: P. Würtz, K. Fredriksson and P. Permi, NMR Laboratory, Institute of Biotechnology, University of Helsinki

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NMR Study of Stereo-Array Isotope-Labeled (SAILed) Proteins: Towards the highthroughput, high-precision structural determinations of larger proteins: Takuya Torizawa 1, Tsutomu Terauchi1, Yuki Iwashita2, Nozomi Sugimori2, Akira M. Ono1, Seiji Tsuchiya1, Mayuri Tai1, Peter Güntert3 and Masatsune Kainosho1, 2, 1CREST/JST, 2Graduate School of Science, Tokyo Metropolitan University, 3RIKEN GSC Implementation of parallel search algorithms using spatial encoding by nuclear magnetic resonance: Rangeet Bhattacharyya, Ranabir Das, K. V. Ramanathan, Anil Kumar, NMR Quantum Compuation and Quantum Information Group, Department of Physics and Sophisticated Instruments Facility, Indian Institute of Science, Bangalore, 560012, India Some Recent Methodological developments in NMR of oriented molecules: Raghav G. Mavinkurve1, Vinay Deepak1, Anu Joy2, N. Suryaprakash2 and K.V. Ramanathan2 , 1Department of physics and 2Sophisticated Instruments Facility, Indian Institute of Science, Bangalore 560 012 Investigation of a dipolar coupled 8-qubit system for Quantum Information processing by NMR: Ranabir Das, Rangeet Bhattacharya and Anil Kumar , NMR Quantum Computation and Quantum Information Group, Department of Physics and Sophisticated Instruments Facility, Indian Institute of Science, Bangalore-560012, India
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C R1ρ Relaxation Experiments Sampling μs Timescale Dynamics of Methyl Groups in Proteins: Ulrika Brath†, Mikael Akke†, Lewis E. Kay ‡, Frans A. A. Mulder†, †Department of Biophysical Chemistry, Lund University, Lund, Sweden, ‡Protein Engineering Networks of Excellence and Departments of Medical Genetics, iochemistry, and Chemistry, The University of Toronto, Toronto, Ontario M5S 1A8, Canada Residual dipolar oscillations in articular cartilage: Sarma V. S. Akella1,2, Ravinder R. Regatte2, Ravinder Reddy2, 1NMR Center, Indian Institute of Chemical Technology, Hyderabad, India, 2 MMRRCC, Department of Radiology, University of Pennsylvania, Philadelphia, PA, USA Measurements of Long-range Residual 1HN-13C Dipolar Couplings in Perdeuterated Proteins: P.R. Jensen1, S. Meier1, M. Blackledge2 and S. Grzesiek1, 1Department of Structural Biology, Biozentrum, University of Basel, Switzerland, 2Institut de Biologie Structurale, Grenoble, France HaCa dipole-dipole and Ha Curie spin relaxation cross-correlation effects in paramagnetic proteins - towards structural refinement: V. N. Sivanandama, Irena Mateckoa, Lukas Trantireka, Guido Pintacudab, Gottfried Ottingc and Norbert Müllera, aInstitute of Organic Chemistry, Johannes Kepler University, Linz, Austria, bDepartment of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden; present address: Laboratoire de Chimie, Ecole Normale Superieure, Lyon, France, cResearch School of Chemistry, Australian National University, Canberra, Australia Mapping Protein-Protein Interactions by Solvent Exposed Amides Experiment: Kong Hung. Sze1, Donghai Lin2, Xuehui Liu3, Yinhua Yang1, Xiao Guan1 and Guang Zhu3, 1 Chemistry Department, Hong Kong University, Pokfulum Road, Hong Kong, 2 Shanghai Institute of Materia Medica, Shanghai 3 Biochemistry Department, HKUST, Hong Kong Combined Computational and Experimental Developments for Automated Determination of Protein Structures by NMR: Kong Hung Sze1, Yinhua Yang1, Xiao Guan1, Man Kit Tse1 and Igor Barsukov2, 1 Chemistry Department, Hong Kong University, Pokfulum Road, Hong Kong, 2 Biological NMR Center, University of Leicester, United Kingdom Cross-correlated relaxation evidence for weak intramolecular hydrogen bonds in solution: Arunima and Narayanan Kurur*, Department of Chemistry, IIT Delhi, Hauz Khas, New Delhi 110016

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Combined MRI and Optical Imaging of Vascular and Extravascular Transport Events in Solid Tumors: Arvind P. Pathak, Ph.D.1, Dmitri Artemov, Ph.D.1, David G. Jackson, Ph.D.2, Michal Neeman, Ph.D.3 and Zaver M. Bhujwalla, Ph.D.1, 1Department of Radiology, The Johns Hopkins University School of Medicine, Baltimore, MD, USA, 2MRC Human Immunology Unit, Weatherall Institute of Molecular Medicine, John Radcliffe Hospital, Oxford, UK, and 3 Department of Biological Regulation, Weizmann Institute of Science, Rehovot, Israel A Novel Filtering Technique Utilized for Aliased Peaks: Chojiro Kojima1, 1Nara Institute for Science and Technology, Nara, Japan Rotating frame experiments for NMR quantum computing: N. Ananth, V. Vimalan and N. Chandrakumar, Department of Chemistry, Indian Institute of Technology-Madras, Chennai – 600 036 Exchange spectroscopy: An approach involving modulated shaped RF pulses: V. Vimalan, S. Pal and N. Chandrakumar, Department of Chemistry, Indian Institute of Technology-Madras, Chennai – 600 036, Tamil Nadu, India NMR-Based Structural Genomics at the Pacific Northwest National Laboratory: Michael A. Kennedy, Pacific Northwest National Laboratory, Biological Sciences Division, EMSL 2569, K898, Richland, WA 99352 USA FT-NMR STUDY OF WATER SOLUBLE FULLERENE DERIVATIVES: RACHANA SINGH+, SANJAY KANOJIA++, AJIT SRIVASTAVA++, T.H. GOSWAMI+, D.N. TRIPATHI++, + ELECTRONIC & SMART MATERIALS / ++CENTRAL ANALYTICAL FACILITY DIVISION, DEFENCE MATERIALS & STORES RESEAECH & DEVELOPMENT ESTABLISHMENT, DMSRDE P.O., G.T. ROAD, KANPUR – 208013 Measurement of 1J(Ni, Ci), 1J(Ni, C’i-1), 2J(Ni, Ci-1), 2J(HNi, C’i-1) and 2J(HNi, Ci) values in 13 C/15N labeled proteins: Sulakshana Mukherjee, Sourajit M. Mustafi, H.S Atreya, and K.V.R Chary, Department of Chemical Sciences, Tata Institute of Fundamental Research, Mumbai 400 005, India Localization Of Nanoscale Magnetic Domains By Magnetic Force Microscopy: Mayur Savla, Denis V. Pelekhov, Camelia Selcu, Petra Schmalbrook, Chris Hammel, Michael Knopp and Gunjan Agarwal, Ohio State University, Columbus, OH, USA Structure Analysis of Chlorosomal Bacteriochlorophyll c Assembly and Chlorosomes by Solid-state NMR: Ayako Egawa 1 , Kengo Akiba 1, Yoshinori Kakitani 2, Yasusyi Koyama 2 , Toshimichi Fujiwara 1 and Hideo Akutsu 1 , 1 Institute for Protein Research, Osaka University, 2 Faculty of Science and Technology, Kwansei Gakuin University Proton-Carbon Correlation Studies of Enantiomers Oriented in Chiral Nematics: H.S.Vinay Deepak1 and K.V.Ramanathan2, 1 Physics Department, Indian Institute of Science, Bangalore, India, 2 Sophisticated Instruments Facilty, Indian Institute of Science, Bangalore, India Homonuclear Correlation Experiments for Half-integer Spin Quadrupolar Nuclei: T.G. Ajithkumar 1, T. Anupõld 2 , A.Samoson 2, E.R.H. van Eck 3 and A.P.M. Kentgens 3, 1 Central NMR Facility, National Chemical Laboratory, Pune 411 008, India, 2 National Institute for Chemical Physics and Biophysics, Academia Tee 23, Tallinn, Estonia, 3 Department of Physical Chemistry / Solid-State NMR, Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands Deuterium Correlation Studies in Solids: Jayanthi.S$, Bibhuti Das$, and K.V.Ramanathan*, $ Department of Physics.,Indian Institute of Science,Bangalore 560012, India, *Sophiticated Instruments Facility,Indian Intitute of Science,Bangalore 560012, India

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Heteronuclear Dipolar Decoupling Effects in Multiple-Quantum and Satellite-Transition Magic-Angle Spinning: S. Ganapathya, J. -P. Amoureuxb, L. Delevoyeb, and P. K. Madhuc, aSolid State NMR Group, National Chemical Laboratory, Pune 411 008, India, bCNRS-8012, ENSCLUSTL, 59652 Villeneuve d’Ascq, France, cDept. of Chemical Sciences, TIFR, Colaba, Mumai 400 005, India Expressed Protein Ligation to Study the Rhodopsin/G-Protein Interface: Insights from High-Resolution Solution NMR: L.L. Anderson1, S.O. Smith2, T.J. Baranski1, G.R. Marshall1, 1 Washington University, Missouri; 2SUNY Stony Brook, New York, USA Application of the wheat germ cell-free protein synthesis system to the structural and functional analysis of proteins with multidimensional NMR spectroscopy: M. Shimizu1, T. Ogasawara1, Y. Endo1, R. Tanaka2, T. Kohno2, E.H. Morita1, 1Ehime University, Ehime, Japan, 2 Mitsubishi Kagaku Institute of Life Sciences, Tokyo, Japan NMR Structure of the N-terminal Domain of SUMO Ligase PIAS1 and Its Interactions with regulatory Factors and DNA: S. Okubo1, F. Hara1, Y. Tsuchida1, S. Shimotakahara1,2, S. Suzuki2, H. Hatanaka3, S. Yokoyama2,4, H. Tanaka1, H. Yasuda1 and H. Shindo1,2, 1Tokyo University of Pharmacy & Life Science, Hachioji, Tokyo 192-0392, Japan, 2RIKEN GSC, Tsurumi-ku, Yokohama 230-0045, 3Kyushu University, Hakozaki, Fukuoka 812-8581, and 4the University of Tokyo, Bunkyo-ku, Tokyo 110-0033 Structural Proteomics: Toward High-Throughput Structural Biology as a Tool in Functional Genomics: Adelinda Yee , Bin Wu, and Cheryl H. Arrowsmith, Ontario Cancer Institute and Department of Medical Biophysics, and Department of Medical Genetics, University of Toronto, 200 Elizabeth Street, Toronto, ON, Canada M5G 2C4

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Molecular mechanism responsible for control of the redox potential of P. Aeruginosa cytochrome c551 revealed by paramagnetic 1H NMR and electrochemical studies: Shin-ichi J. Takayama,1 Shin-ichi Mikami,1 Norifumi Terui,1 Hajime Mita,1 Jun Hasegawa,2 Yoshihiro Sambongi,3 and Yasuhiko Yamamoto1, 1 Graduate school of pure and applied sciences, University of Tsukuba, Tsukuba 305-8571, Japan, 2 Daiichi Pharmaceutical Co., Ltd., Edogawa-ku, Tokyo 134-8630, Japan, 3 Graduate School of Biosphere Science, Hiroshima University, HigashiHiroshima 739-8528, Japan Solution Structure Calculation Of Two Hypothetical Proteins From Pseudomonas Aeruginosa Genome: Sampath Srisailam and Cheryl Arrowsmith, Clinical Genomic Center, University Health Network, Toronto, Ontario, Canada Structural studies on the C-terminal peptides of glycosomal Phosphoglycerate Kinase from Leishmania mexicana: Vidya Raghunathan, Sangita Aggarwal, National Institute of Immunology, Aruna Asaf Ali Marg, N.Delhi – 110067, INDIA GYF domain proteomics: Michael Kofler1 and Christian Freund1, 1Protein Engineering Group, Forschungsinstitut für Molekulare Pharmakologie und Freie Universität Berlin, Robert-RössleStr. 10, 13125 Berlin,Germany Structure-Functional Relation of a Novel Calcium Binding Protein from Entamoeba histolytica: Ritu Bansal-Mutalik1, Sourajit M. Mustafi1, Paramita Chakrabarty2, Alok Bhattacharya2 and Kandala V.R. Chary1 , 1Department of Chemical Sciences, Tata Institute of Fundamental Research, Mumbai, India, 2School of Environmental Sciences and School of Life Sciences, Jawaharlal Nehru University, New Delhi, India p53 Dimerization Mutants Lack DNA Binding by Missing Cooperativity: A. Dehner,1 C. Klein,2 S. Hansen,2 M. Schwaiger,2 H. Kessler,1 1Department Chemie, Technische

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Universität München, 85747 Garching, Germany, 2Pharma Research, Roche Diagnostics GmbH, 82372 Penzberg, Germany P40 NMR structural studies on a hypothetical protein, YKR049C derived from Saccharomyces cerevisiae: Jinwon Jung1, Cheol-Jin Lee1, Adelinda Yee2, Cheryl H. Arrowsmith2 and Weontae 1 1 Lee , Department of Biochemistry, Yonsei University, Seoul, Korea, 2Ontario Cancer Institute, University of Toronto, Toronto, Canada Distributed Computing and NMR Constraint-Based Protein Structure Determination: Applied for Endothelin-1 and Holo-neocarzinostatin: H. Takashima,1 T. Yoshida,2 T. Ishino,2 K. Hasuda,3 N. Mimura,1 Y. Nishi,2 T. Ohkubo,2 Y. Kobayashi,2 1Novartis Institutes for BioMedical Research, Tsukuba, 2Osaka University, Osaka, 3POLA Chemical Industries Inc., Japan

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PROTEIN STRUCTURE, INTERACTION & DYNAMICS P42 Structural survey of the La autoantigen: insights into RNA recognition:D. Sanfelice1, C. Alfano1, J. Babon2, G. Kelly3, S. Curry4 and Maria R Conte1, 1Biophysics Laboratories, IBBS, University of Portsmouth, Portsmouth PO1 2DT, UK, 2Department of Molecular structure, Walter and Eliza Hall Institute, Vic 3052, Australia, 3Biomedical NMR Centre, National Institute for Medical Research, London NW7 1AA, UK, 4Department of Biological Sciences, Imperial College London, SW7 2AZ, UK NMR Structure of a Type IVb Pilin from Salmonella typhi and Its Assembly into Pilus: Xing-Fu Xu,1 Yih-Wan Tan,1 Lam Lam,2 Jim Hackett,2 Mingjie Zhang,2 and Yu-Keung Mok,1 1 Department of Biological Sciences, National University of Singapore, Singapore 117543, 2 Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Hong Kong Water in hydrophobic cavities in proteins: a computational study: Chandra Verma, Computational Biology, Bioinformatics Institute, Biopolis, Singapore-138671 Determination of the Binding Specificity of the 12S and 5S Subunits of the Transcarboxylase by Saturation Transfer Difference NMR: Rakesh Bhat, Claudia Peikert, Karsten Seeger and Stefan Berger, Institut für Analytische Chemie, Universität Leipzig, Johannisallee 29, D-04103 Leipzig, Germany The tetrameric L27 domain complex as an organization platform for supramolecular assemblies: Wei Feng1, Jia-Fu Long1, Jing-Song Fan1, Tetsuya Suetake1, and Mingjie Zhang1, 1 Department of Biochemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, China Molecular architecture of the insulin-like growth factor binding proteins (IGFBPs): Sudipta Majumdar, Madhumita Ghosh, Igor Siwanowicz, Loyola D’Silva, and Tad A. Holak, Max Planck Institute for Biochemistry, D‑ 82152 Martinsried, Germany Molecular determinants for complex formation between the retinoblastoma protein and the LXCXE sequence containing proteins: Mahavir Singh, Marcin Krajewski, and Tad A. Holak, Max Planck Institute for Biochemistry, D-82152 Martinsried, Germany NMR Structural Studies on DdCAD-1: a Ca2+-dependent Cell-Cell Adhesion Molecule: Zhi Lin1, Eric Huang2, Chi-Hung Siu2, Daiwen Yang1, 1 Dept of Bio Sci, National University of Singapore, Singapore, 2Banting and Best Department of Medical Research and Department of Biochemistry University of Toronto,Toronto, Ontario M5G 1L6, Canada

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Lipid bilayer triggers the release of chromophore from neocarzinostatin: Hariharan Parameswarana,b, Shan-Ho Choub, Der-Hang China*, aDepartment of Chemistry, National Chung Hsing University, Taichung, Taiwan, ROC.; bInstitute of Biochemistry, National Chung Hsing University, Taichung, Taiwan, ROC Nickel binding to histone H4: Maria Antonietta Zoroddua, Massimiliano Peanaa, Serenella Medicia, Max Costab, aDepartment of Chemistry & Faculty of Pharmacy, University of Sassari, Italy, bDepartment of Environmental Medicine, N.Y . University, School of Medicine, USA Nickel binding in the C-terminal domain of Cap43 protein: Maria Antonietta Zoroddua, Massimiliano Peanaa, Serenella Medicia, Teresa Kowalik-Jankowskab, Henryk Kozlowskib, Max Costac, aDepartment of Chemistry, University of Sassari, Sassari, Italy, bFaculty of Chemistry, University of Wroclaw, Po; cDepartment of Environmental Medicine, New York University, USA NMR and biophysical studies on the periplasmic domain of Escherichia coli sensor histidine kinase EnvZ: Ahmad Khorchid1, Masayori Inouye2, and Mitsuhiko Ikura1, 1Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario, M5G 2M9, Canada, 2Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA Tracking NMR-defined exchange motions across the folding-unfolding equilibrium of horse ferricytchorme c: D. Krishna Rao,* S. Satyanarayana and Abani K. Bhuyan, University of Hyderbad, School of Chemistry, Hyderbad 500 046 Structure and Interactions of the Malarial Surface Antigen AMA1: R.S. Norton,1 Z.P. Feng,1 R.A. Evans-Stevenson,1 D.W. Keizer,1 S. Yao,1 A. Coley,2,3,4 M. Foley,2,3 R.F. Anders2,4, 1 Walter and Eliza Hall Institute of Medical Research, Parkville 3050, Australia, 2 Department of Biochemistry, La Trobe University, Bundoora 3083, Australia, 3 CRC for Diagnostics and 4 CRC for Vaccine Technology, Bundoora 3083, Australia C-Terminal Domain of Insulin-Like Growth Factor (IGF) Binding Protein-6. Implications for Regulation of IGF Action: R.S. Norton,1 S.J. Headey,1,2 D.W. Keizer,1 S. Yao,1 L.A. Bach2, 1 Walter and Eliza Hall Institute of Medical Research, Parkville 3050, Australia, 2 Department of Medicine, University of Melbourne, Austin Hospital, Heidelberg 3084, Australia NMR snap shots of a fluctuating ubiquitin structure at 30 bar-3kbar: Ryo Kitahara1, Shigeyuki Yokoyama12,3,4, Kazuyuki Akasaka1,5, 1Structural and Molecular Biology Lab., 2 Structurome Research Group, RIKEN Harima, 3RIKEN Genomic Science Center, 4Department of Biophisics and Biotechnology, University of Tokyo, 5Department of Biotechnological Science, Kinki University Solution structural studies on E.coli pantothenate synthetase using NMR methods: Kalyan Sundar Chakrabarti and Siddhartha P. Sarma, Molecular Biophysics Unit, Indian Institute of Science, Bagalore-560012 Rational Design of Akt Specific Inhibitors: Christian Roumestand, Daniel Auguin, Virginie Ropars, and Masayuki Noguchi, Centre de Biochimie Structurale, Faculte de Pharmacie, Montpellier France, Division of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Japan TROSY-NMR and Saturation Transfer Studies of Calmodulin Complexed with Intact Human Lactoferrin: H. Ishida1 and H. J. Vogel1, 1University of Calgary, Alberta, Canada Biophysical characterization of a molten globular affibody: C. Lendel,1 V. Dincbas-Renqvist,1 A. Flores,2 E. Wahlberg,1 J. Dogan,1 T. Härd3, 1 Royal Institute of Technology (KTH), Stockholm, Sweden, 2 Umeå University, Umeå, Sweden, 3 Göteborg University, Göteborg, Sweden

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Conformations of Nucleotides Bound to Wild Type and Y78F Mutant Yeast Guanylate Kinase: Proton Two Dimensional Transferred NOESY Measurements: Bruce D. Ray1, Gotam K. Jarori2, Honggao Yan3, Vidya Raghunathan4, and B.D. Nageswara Rao1, 1Department of Physics, Indiana University - Purdue University at Indianapolis (IUPUI), Indiana, USA, 2Tata Institute of Fundamental Research, Mumbai, India, 3Department of Biochemistry Michigan State University, East Lansing, MI, USA, 4National Institute of Immunology, New Delhi, India Structural Basis of Myosin Phosphatase Inhibitory Protein, CPI-17: S.Ohki1, F.Matsuzawa2, K.Yokota1, and M.Eto3, 1Japan Advanced Institute of Science and Technology (JAIST), 2Celester Lexico-Sciences, 3Univ. of Virginia NMR studies on the 56kDa Escherichia coli nickel-binding protein NikA: Sundaresan Rajesh1,2,3,4, Kaori Kurashima1,2,5 , Daniel Nietlispach6, Masahiro Shirakawa7, Jonathan Heddle3, Jeremy Tame3 and Yutaka Ito1,2,5, 1Research Group for Bio-supramolecular Structure-Function, RIKEN, JAPAN; 2Molecular and Cellular Physiology, 3Protein Design, and 7Molecular Biophysics Laboratories, Graduate School of Integrated Science, Yokohama City University, JAPAN; 4Division of Cancer Studies, School of Medicine, University of Birmingham, UK; 5 CREST, JST, JAPAN; 6Department of Biochemistry, University of Cambridge, UK Structural features of Neurokinin-2 Receptor Selective Peptide Agonists and their role in receptor selectivity: Indu R.Chandrashekar1, M. Anil Kumar1, Anjali Dike1, Sudha M.Cowsik1 and Gita Subha Rao2, 1School Of Life Sciences, Jawaharlal Nehru University, New Delhi, India-110067, 2Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India Structural characterization of Scyliorhinin I: A dual NK1/NK2 receptor agonist: Anjali Dike, Indu Chandrashekar, Anil Mantha and Sudha M Cowsik, Jawaharlal Nehru University, New Delhi-67, INDIA Investigation of the protein with the help of multidimensional NMR spectroscopy: M. D. Mukrasch1, M. Zweckstetter1, C. Griesinger1, M. von Bergen2, J. Biernat2, E.-M. Mandelkow2, E. Mandelkow2, 1Max-Planck-Institute for biophysical chemistry, Göttingen, 2Max-PlanckArbeitsgruppen für strukturelle Molekularbiologie Hamburg Conformational analysis of HIV Rev protein in solution at acidic pH: Daniel Padró and Francisco Blanco, Structural and Computational Biology Programme, Centro Nacional de Investigaciones Oncológicas Melchor Fernández Almagro 3, 28029 Madrid, Spain NMR Structural Studies of the Interferon α Signaling Complex: Sabine R. Quadt1, Jordan H. Chill1, Rina Levy1, Jacob Piehler2, Jacob Anglister1, 1Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel; 2Institute of Biochemistry, Johann Wolfgang Goethe University Frankfurt am Main, Germany Residual Dipolar Couplings and some specific Models for Motional Averaging: M. Deschamps,1 I.D. Campbell,1 J. Boyd1, 1Oxford University, United Kingdom Probing Protein-Peptide Binding Surfaces Using Charged Stable Free Radicals and Transverse Paramagnetic Relaxation Enhancement (PRE):M. Deschamps,1 E.S. Pilka,1 J.R. Potts,1 I.D. Campbell,1 J. Boyd1, 1Oxford University, United Kingdom Sorting out a sortase: characterizing the substrate binding site of sortase A from Staphyloccocus aureus: C.K. Liew1, N. Suree1, B.T. Smith1, M.T. Naik1, R. Pilpa1, U. Ilangovan1, M.E. Jung1, R.T Clubb1, 1Department of Chemistry and Biochemistry, University of California, Los Angeles

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NMR Structure Studies of an Anion Binding Channel-Forming Heptapeptide: Gabriel A. Cooka, Mahalaxmi Aburib, Paul E. Smithb, John M. Tomicha, Robert Pajewskic, Paul H. Schlesingerc, George W. Gokelc, aDepartment of Biochemistry Kansas State University, Manhattan, KS 66506, bDepartment of Chemistry Kansas State University, Manhattan, KS 66506, c Department of Molecular Biology & Pharmacology, Washington University School of Medicine, St. Louis, MO 63110 Towards the solution structure of a 34 kDa ternary complex involved in bacteriophage Lambda recombination: M.D. Sam1, E.A. Fadeev1, C.V. Papagiannis2, R.C. Johnson2 and R.T. Clubb1, 1Department of Chemistry and Biochemistry, University of California, Los Angeles, USA, 2 Department of Biological Chemistry, UCLA School of Medicine, USA Solution structure of the DNA binding domain A of Saccarimyces cerevisiae RPA and its interaction with single stranded DNA: Chin-Ju Park1, Joon-Hwa Lee2, Mi-Kyung Lee1, Sung Jae Cho1 and Byong-Seok Choi1, 1Department of Chemistry and National Creative Research Initiative Center, Korea Advanced Institute of Science and Technology, Korea, 2Department of Chemistry and Biochemistry, University of Colorado at Boulder, USA Solution Structural Studies of Regulatory Subunit of Acetohydroxy Acid Synthase: Ashima Mitra1 and Siddhartha.P.Sarma1, 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore Mapping the Binding Interface of XPF-ERCC1 complex by Cross-saturation Experiment: Yun-Jeong Choi, Mi-Kyung Yoon, Seikh Imtiaz Ali and Byong-Seok Choi, Department of Chemistry, Korea Advanced Institute of Science and Technology, 373-1, Guseong-dong, Yuseonggu, Daejon, 305-701, Korea 3D Structure Of Elderberry Lectin and its Unexpected EL:N,N',N''-Triacetylchitotriose 2:1 Binding Ratio: C. Mihai15, L. Buts2, L. Wyns2, W. J. Peumans3, E. J. M. Van Damme4, J. C. Martins1 and R. Willem5, 1Eenheid NMR en Structuuranalyse, Universiteit Gent, Belgium, 2Dienst Ultrastructuur, VIB, Vrije Universiteit Brussel, Belgium, 3Laboratory for Phytopathology and Plant Protection, Katholieke Universiteit Leuven, Belgium, 4Vakgroep Moleculaire Biotechnologie, Universiteit Gent, Belgium, 5HNMR Centre and POSC, Vrije Universiteit Brussel, Belgium Danger, Homo-dimer : M. Coles, S. Djuranovic, M. Hulko, A.N. Lupas, Max-Planck-Institute for Developmental Biology, TŸbingen, German Solution NMR Studies of Holo form of Plasmodium falciparum Acyl Carrier Protein: Alok Kumar Sharma1, Shailendra Kumar Sharma1, Rahul Modak2, Namita Surolia2, Avadhesha Surolia1 and Siddhartha P. Sarma1, 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore 560012, 2Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur,Bangalore 560064 Kinetics and Mechanism of Microsecond Conformational Changes in Plastocyanin Induced by Histidine Protonations: A 15N Relaxation Study: Mathias A. S. Hass1, Marianne H. Thuesen2, Hans E. M. Christensen2,Jens J. Led1, 1 Department of Chemistry, University of Copenhagen, Universitetsparken 5, DK-2100 Copenhagen, Denmark, 2 Department of Chemistry, The Technical University of Denmark, Building 207, DK-2800 Lyngby, Denmark Solution Structure of Sterile Alpha Motif (SAM) Domain of Deleted in Liver Cancer-1 (DLC-1): Shuai Yang, Jingfeng Zhang, Boon Chuan Low, Daiwen Yang, Department of Biological Sciences and Department of Chemistry, National University of Singapore, 14 Science Drive 4 Singapore 117543

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Eukaryotic Translation Termination Factor GSPT/eRF3 Recognizes PABP with Chemical Exchange Using Two Overlapping Motifs: M. Osawa1, T. Nakanishi1, S. Hoshino1, T. Katada1, and I. Shimada1,2, 1Grad. Sch. of Pharm. Sci., The Univ. of Tokyo, Tokyo, Japan; 2BIRC, Tokyo, Japan The solution structure of the DNA binding domain of NikA: H. Yoshida1, N. Furuya1, Y.J. Lin2, T. Komano1, P. Güntert2, M. Kainosho1, 1CREST/JST and Tokyo Metropolitan University, Tokyo, Japan, 2RIKEN Genomic Sciences Center, Yokohama, Japan NMR studies on the sensory domain of the two component Histidine kinases , DcuS and CitA: Vinesh Vijayan1 , Michael Bott2, Gottfried Unden3, Markus Zweckstetter1, and Christian Griesinger1, 1Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany,2 Institut für Biotechnologie 1, Forchungszentrum Jülich, D-52425 Jülich, Germany,3Institut für Microbiologie und Weinforschung, Universität Mainz, Becherweg 15, D55099 Mainz, Germany Solution Structure of the Replication Initiator Protein Nuclease Domain from a Nanovirus: Ramón Campos-Olivas and Susana Vega, CNIO (Spanish National Cancer Center), Madrid, Spain NMR structure determination of mouse Apolipoprotein AI/prebHDL Particles: Arun Sivashanmugam1, Xuefeng Ren1, Leslie Korando1, Lei Zhao1, Qianqian Li1, Daniel Sparks2 & Jianjun Wang1, 1 Department of Biochemistry and Molecular Biology and Department of Anatomy, Southern Illinois University, Carbondale, Illinois, USA, 62901- 4413, 2 Heart Institute, University of Ottawa, Ottawa, Ontario, CANADA Structural Basis for the cyclic AMP Signal Translation in PKA by NMR: Rahul Das2, Veronica Esposito2, Bart Kalata2, S. Brown1, T. Sjoberg1, D. J. Vigil1, S. S. Taylor1, G. Melacini2*, 1 University of California, San Diego, USA, 2 McMaster University, Hamilton, Ontario, Canada Protein Dynamics Play a Key Role in Determining the Specific Recognition of GU-rich polyadenylation regulatory elements by human Cstf-64 protein: Pritilekha Deka, P. K. Rajan, Jose’ Manuel Perez-Canadillas1 and Gabriele Varani*, Department of Biochemistry and Department of Chemistry, University of Washington, Seattle Washington 98195-1700, USA, 1MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH England NMR analysis of human mitochondrial ABC transporter, ABCB6: Kaori Kurashima1,2,3 Hiroshi Sembongi3,4, Takehiko Shibata1,2,3 and Yutaka Ito1,2,3, 1Research Group for Biosupramolecular Structure-Function, RIKEN, JAPAN; 2CREST, JST, JAPAN;, 3Molecular Biophysics Laboratories, Graduate School of Integrated Science, Yokohama City University, JAPAN; 4Mitochondrial Diseases Group, MRC Dunn Human Nutrition Unit, UK Structural and functional analyses of Thermus thermophilus RecO: Jin Inoue1,2, Masayoshi Honda1,2,3, Takehiko Shibata1,2,4, Yutaka Ito1,2,3, and Tsutomu Mikawa1,2,3,4, 1Graduate School of Integrated Science, Yokohama City University,Japan; 2Research Group for Bio-supermolecular Structure Function and 4Structurome Research Group, RIKEN, Japan; 3CREST/JST Molecular mechanism of RecR-DNA interactions: Masayoshi Honda1,2,3, Jin Inoue1,2, Yosimasu Masatoshi1,3, Tsutomu Mikawa1,2,3,4, Takehiko Shibata1,2, and Yutaka Ito1,2,3, 1Research Group for Bio-supramolecular Structure-Function RIKEN, JAPAN; 2Molecular and Cellular Physiology Laboratory, Graduate School of Integrated Science, Yokohama City University, JAPAN; 3 CREST/JST; 4Structurome Res. Group, RIKEN, JAPAN The Solution Structure of the FATC Domain of the Protein Kinase TOR Suggests a RedoxDependent Regulatory Mechanism: Sonja A. Dames1, Jose M. Mulet2, Klara Rathgeb-Szabo1,

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Michael N. Hall2, & Stephan Grzesiek1, 1Department of Structural Biology, 2Department of Biochemistry, Biozentrum, University of Basel, Switzerland P94 Structure and Dynamics Characterization of Protein Domains in the Transacylase Component of Human Mitochondrial Branched-Chain Ketoacid Dehydrogenase: Chi-Fon Chang1, Yi-Jan Lin2, Hui-Ting Chou3, Shin-Jye Lee3, David T. Chuang4, Tai-Huang Huang1,3, 1 Gemomics Research Center, Academia Sinica, Nan-Kang, Taipei 11529, Taiwan, 2RIKEN Genomic Sciences Center, Yokohama 230-0045, Japan, 3Institute of Biomedical Sciences Academia Sinica, Nan-Kang, Taipei 11529, Taiwan, 4Dept of Biochemistry, U. of Texas Southwestern Medical Center, Dallas, Texas Physical Properties of Spider Dragline Silk Investigated by Solid-State NMR Spectroscopy: Isabelle Marcotte1, Fritz Vollrath2 and Beat H. Meier1, 1Department of Physical Chemistry, ETHHönggerberg, CH-8093, Zürich, Switzerland, 2Department of Zoology, Oxford University, OX1 3PS Oxford, United Kingdom Cryptic vinculin binding sites in the talin rod : Ian Fillingham, Alexandre R. Gingras, Bipin Patel, Jonas Emsley, David R. Critchley, Gordon C.K. Roberts and Igor L. Barsukov, Biological NMR Centre, University of Leicester, University Road, Leicester, LE1 7RH, UK Role of Neurokinin B and Ab-protein fragment 25-35 on aging rat brain synaptosomes: Anil K Mantha, Indu R. Chandrashekar, Anjali Dike, K. Moorthy, Najma Z. Baquer and Sudha M. Cowsik, School of Life Sciences, Jawaharlal Nehru University, New Delhi – 110 067, INDIA GTPase Effector Domain of Dynamin: structure function relationships: Jeetender Chugh1, Amarnath Chatterjee1, Ashutosh Kumar1, Ram Kumar Mishra2, Rohit Mittal2, and Ramakrishan V. Hosur1, 1Departments of Chemical and 2Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumabi 400005, India Conformation and Dynamics of Protein L12 in Solution and on the Ribosome: Frans A. A. Mulder, Lamine Bouakaz, Anna Lundell, Musturi Venkataramana, Anders Liljas, Suparna Sanyal and Mikael Akke, Departments of Biophysical Chemistry & Molecular Biophysics, Lund University, Sweden, & Department of Cell and Molecular Biology, BMC, Uppsala University, Sweden Structural Characterization of Filamin Repeat 21 And its Interaction With Migfilin: S. S. Ithychanda1, X. Wang1, Y. Xu1, C. Wu2, J, Qin1, 1Cleveland Clinic Foundation, Cleveland, USA, 2 University of Pittsburgh, Pittsburgh, USA Protein Structure from Residual Dipolar Couplings and Minimal NOE Information using Molecular Fragment Replacement: Georg Kontaxis1, Zhengrong Wu2, Frank Delaglio3 and Ad Bax3, 1Department of Structural Biology, Vienna University, Austria, 2Department of Biochemistry, Ohio State University, OH, USA, 3NIDDK, NIH, Bethesda, MD, USA Heteronuclear NMR Investigations of Dynamic Regions of Intact E. coli Ribosomes: John Christodoulou*, Göran Larsson*,, Paola Fucini†, Kresten Lindorff-Larsen*, Michele Vendruscolo*, Christina Redfield‡, Jürgen Schleucher¶ and Christopher M. Dobson*, *Department of Chemistry, University of Cambridge, Cambridge, UK, † Max-Planck-Institute für Molekulare Genetik, Berlin, Germany, ‡ Oxford Centre for Molecular Sciences, University of Oxford, Oxford, UK, ¶ Department of Medical Biochemistry and Biophysics, Umeå University, Umeå, Sweden Solution Structure of a Vanadium-binding Protein, Vanabin2 from the Vanadium-rich Ascidian, Ascidia sydneiensis samea: Toshiyuki Hamada1,2, Miwako Asanuma1, Tatsuya 3 1 Ueki , Fumiaki Hayashi , Naohiro Kobayashi1, Shigeyuki Yokoyama1, Hitoshi Michibata3,

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Hiroshi Hirota1,2 , 1 RIKEN Genomic Sciences Center, Yokohama, JAPAN, University, Yokohama, JAPAN, 3 Hiroshima University, Hiroshima, JAPAN P104

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Characterization of magnesium-binding site in the calcium-binding photoprotein aequorin by NMR analysis: Wakana Ohashi1, Satoshi Inouye2, Toshio Yamazaki1, Yukiko DoiKatayama1, higeyuki Yokoyama1, Hiroshi Hirota1, RIKEN Genomic Sciences Center, Yokohama, JAPAN, Yokohama Research Center, Chisso Corporation, Yokohama, JAPAN MR Studies of Activating Domain of Transcription Factor Hex with GST: A. Sakurai1, D. A. remu1, J. Kurita2, T. Noguchi3, S. Meshitsuka1, 1Tottori Univ., Tottori, 2Varian Inc., 3Nagoya niv., Nagoya, Japan Structural characterisation by NMR of bioengineered cyclic peptides for the treatment of multiple sclerosis: Masa Cemazar1, Claude Bernard2 and David Craik1, 1Institute for Molecular Bioscience, University of Queensland, Brisbane, Australia, 2Neuroimmunology Laboratory, La Trobe University, Melbourne, Australia Histidine residues are essential for optimal metal binding to bacterial metallothionein: Claudia A. Blindauer1,2, M. Tahir Razi1,3, Dominic J. Campopiano1 and Peter J. Sadler, 1University of Edinburgh, UK; 2University of Warwick, UK; 3Bahauddin Zakariya University, Multan, Pakistan NMR Evidence for Enzyme-Induced Strain in the Michaelis Complex of Serine Protease from SGNH-hydrolase Family with Paraoxon: Mechanism of Initial Noncovalent Binding: Sergiy I. Tyukhtenko1, Ching-Yu Chou1, Chi-Fon Chang2, Tai-Huang Huang1,2, 1Institute of Biomedical Sciences, Academia Sinica, Nan-Kang, Taipei 11529, Taiwan, 2Genomics Research Center, Academia Sinica, Nan-Kang, Taipei 11529, Taiwan NMR Solution Structure Investigation of the Mitochondrial Protein Import Receptor Tom20 from Arabidopsis thaliana: Henrik Biverståhl, Anna-Karin Berglund, Elzbieta Glaser and Lena Mäler, Stockholm University, Sweden Combined MD and NMR Analysis of Short Peptides: J. Graf1*, P. Nguyen2*, Y. Mu2, G. Stock2, H. Schwalbe1, 1 Institute of Organic Chemistry and Chemical Biology, 2 Institute of Physical and Theoretical Chemistry, J. W. Goethe-University Frankfurt a. M., Germany Analysis of DNA and ATP binding sites in the central domain of RecA using multidimensional NMR spectroscopy: Tsutomu Mikawa1, 2, Takehiko Shibata1 and Yutaka Ito1, 2, 1Research Group for Bio-supramolecular Structure-Function, RIKEN, JAPAN, 2CREST, JST
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H, 13C and 31P NMR of inositol 1,4,5-trisphosphate (IP3) in complex with IP3 receptor: Tapas K. Mal1, Ivan Bosanac1, Jenny Chan1, Akira Ono,2 Masatsune Kainosho2, Ad Bax3, Mitsuhiko Ikura1, 1Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario, M5G 2M9, Canada, 2Department of Chemistry Faculty of Science, Tokyo Metropolitan University, 1-1 Minami-oshawa, Hachioji, Tokyo, 192-0397, Japan, 3Laboratory of Chemical Physics, NIDDK, National Institutes of Health, Bethesda, MD 20892-0520, USA Structural Investigations of the Pre-mRNA Processing Protein Prp24 from S. cerevisiae: N.J. Reiter1, S. Kwan2, M. Tonelli3, A. Bahrami3, H. Eghbalnia3, D.A. Brow2, S.E. Butcher1,3, 1 University of Wisconsin-Madison, Department of 1Biochemistry, 2Biomolecular Chemistry, and the 3National Magnetic Resonance Facility at Madison (NMRFAM), Wisconsin, USA

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Characterization of Correlated Chemical Exchange in a C-terminal Calmodulin Mutant using Multiple Quantum Spin Relaxation: Patrik Lundström, Frans A.A. Mulder and Mikael Akke, Department of Biophysical Chemistry, Lund University, Box 124, SE-221 00 Lund, Sweden Structure and function of the C-terminal domain of Abl kinase: Cameron Mackereth1, Oliver Hantschel1, Silke Wiesner1, Thomas Guettler2, Michael Sattler1, Giulio Superti-Furga1, 1European Molecular Biology Laboratory, Heidelberg, Germany, 2Ruprecht-Karls-Universitaet, Heidelberg, Germany Structure and functional analysis of the MYND domain: Roberta Spadaccini1, Matthew Bottomley2, Stephane Ansieu3 & Michael Sattler1, 1EMBL Heidelberg Germany, 2IRBM- Pomezia (Rome) Italy, 3INSERM,ENS-Lyon,France Investigating a large protein by NMR Spectroscopy: E. coli Citrate Synthase: K. Choudhary, J. O’Neil and H.W. Duckworth, University of Manitoba, Winnipeg, Manitoba, Canada NMR Study of the Interaction of the beta-Amyloid Peptide of Alzheimer's Disease with Potential Aggregation-Inhibitors: D. Benaki1, K. Stathopoulou2, M. Pelecanou1, E. Mikros2, 1 Institute of Biology, NCSR “Demokritos” 15310 Athens, Greece, 2Division of Pharmaceutical Chemistry, University of Athens, Panepistimiopolis, Zografou 157 71, Greece NMR studies on the biomolecules: Structural analysis of proteins and peptides: Woo-Sung Son1 Yong-Jin Kim1, Won-Je Kim1, Su-Jin Kang1, Min-duk Seo1, Sung-Jean Park1, Sung-Jean Park1, Bong-Jin Lee1, 1National Research Laboratory for Membrane Protein Structure, College of Pharmacy, Seoul National University, San 56-1, Shillim-dong, Gwanak-gu, Seoul, Republic of Korea Backbone Dynamics of Sortase A and Sortase B in Staphylococcus aureus: 15N Relaxation Study: Pilpa R., Naik M., Liew C, Suree N. and Clubb R* Structure-function studies on binding of Forkhead-Associated domain FHA1 of the DNA damage checkpoint protein Rad53 with the biological and synthetic partners: Anjali Mahajan1, Chunhua Yuan2,3 and Ming-Daw Tsai1,2,3,4,5, 1Biophysics Program, The Ohio State University, 2Campus Chemical Instrument Center, The Ohio State University, 3Department of Chemistry, The Ohio State University, 4Department of Biochemistry, The Ohio State University, 5 Genomics Research Center, Academia Sinica, Taiwan Structure of the pyrin domain from the zebrafish caspase, Caspy: K. Johan Rosengren and Justine M. Hill, Institute for Molecular Bioscience, The University of Queensland, Brisbane QLD 4072, Australia Structure and dynamics of a thermophilic acylphosphatase from Pyrococcus horikoshii by NMR spectroscopy ¨C structural basis of thermostability and enzymatic activities: Kong Hung Sze1, Yinhua Yang1, Xiao Guan1, Man Kit Tse1, K.K. Cheung2 and KamBo Wong2, 1 Chemistry Department, Hong Kong University, Pokfulum Road, Hong Kong, 2 Biochemistry Department, the Chinese University of Hong Kong, Hong Kong Studies of Peptide Hormone/Receptor Interactions by NMR Spectroscopy: N. Tidten1, N. Link1, T. Lauber1, D. Schuster1, K. Vitzithum1, P. Rösch1, U. C. Marx1,2, 1Lehrstuhl für Biopolymere, Universität Bayreuth, 95440 Bayreuth, Germany, 2Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia Methyl dynamics for understanding hydrophobic core packing of dynamically different motifs of dsRBD of PKR: Ravi P. Barnwal, Tista R. Chaudhuri, S. Nanduri and Qin J §, Department of Chemical Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Colaba, Mumbai-400005 and §Cleveland Clinic Foundation, Cleveland OH, USA

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lternative splicing factor ZNF265 and its interaction with RNA: Fionna Loughlina and Joel Mackaya, University of Sydney, NSW, Australia Solution structures of plant telomere binding proteins: S.G. Ko1,3, H.Y. Park1,3, J. Shin1,3, E. Y. Yu2,3, M.G. Hwang3, S.W. Yang3, I. K. Chung2,3, W.T. Kim3, M.H. Cho3 and W. Lee1,3, 1 Department of Biochemistry, 2Department of Biology, College of Science, and 3Protein Network Research Center, Yonsei University, Seoul 120-749, Korea Structure and DNA Binding Mode of C-terminal Domain of Response Regulatory Protein from Helicobacter pylori: Byoung young Jeon1, Eunmi Hong1, Jin-Hwan Kim2 ,Young-Ho Jeon2 and Weontae Lee1, 1Department of Biochemistry and Biomolecular NMR Laboratory, Yonsei University, Seoul 120-749, Korea; 2Crystalgenomics, Inc. Daeduk, Taejon 305-390 Korea Solution structure of a two-component response regulatory protein derived from Helicobacter pylori: Eunmi Hong, Byoung-young Jeon, Joon Shin and Weontae Lee*, Department of Biochemistry and Biomolecular NMR Labortory, Yonsei University, Seoul 120-749, Korea Denaturant Induced Protein Stabilization: A PMRD Study: M. Trivikaram Rao1, A.K. Bhuyan2, K. Venu1 and V.S.S. Sastry1, School of Physics1 and School of Chemistry2, University of Hyderabad, Hyderabad, 500 046, India Structural analysis of scavenger receptor LOX-1 and its interaction with oxidized LDL: I. Ohki, T. Ishigaki, T. Oyama, K. Morikawa, S. Tate, Biomolecular Engineering Research Institute (BERI), Osaka, JAPAN New tools to study protein-ligand interaction by nuclear magnetic resonance spectroscopy: Sridhar Sreeramulu, Thomas Langer, Martin Vogtherr, Ulrich Schieborr and Harald Schwalbe, Institute of Organic Chemistry and Chemical Biology, J. W. Goethe-University Frankfurt a. M., Germany Solution structure of ribosomal protein L16 from Thermus thermophilus HB8: Mitsuhiro Nishimura1, Takuya Yoshida1, Mikako Shirouzu2,3, Takaho Terada2,3, Seiki Kuramitsu3,4 , Shigeyuki Yokoyama2,3,5, Tadayasu Ohkubo1 and Yuji Kobayashi1, 1Graduate School of Pharmaceutical Sciences, Osaka University, Osaka Japan, 2RIKEN Genomic Sciences Center, Yokoyama Japan. 3RIKEN Harima Institute at SPring-8, Hyogo Japan, 4Department of Biology, Graduate School of Science, Osaka University, Osaka Japan, 5Department of Biophysics and Biochemistry, Graduate School of Science, the University of Tokyo, Tokyo, Japan A receptor that directly interacts with small GTPases. NMR structure of the Rac1 binding domain of human plexin-B1 and surface mapping: Yufeng Tong and Matthias Buck, Department of Physiology and Biophysics, Case Medical School, Cleveland, Ohio, USA, 44106 Structure and function of the subdomains of MAP-LC3: T. Kouno1, M. Mizuguchi1, I. Tanida2, T. Ueno2, E. Kominami2, K. Kawano3, 1Toyama Med. Pharm. Univ., Fac. Pharm. Sci., Toyama, Japan, 2Juntendo Univ., Sch. Med., Tokyo, Japan, 3Hokkaido Univ., Grad. Sch. Sci., Sapporo, Japan Solution structure of rice phytochrome B nuclear localize signal domain: Toshitatsu Kobayashi1, Ryo Tabata1, Masaki Mishima1, Kayo Akagi2, Nobuya Sakai2, Etsuko Katoh2, Makoto Takano2, Toshimasa Yamazaki2 and Chojiro Kojima1, 1 Graduate School of Biological Science, Nara Institute of Science and Technology, and 2National Institute of Agrobiological Sciences (NIAS)

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Toward a More Perfect Order: Molecular Geometry of a Membrane-Associating Protein and Its Ligands: Anita I. Kishore, Ronald D. Seidel, and James H. Prestegard, Complex Carbohydrate Research Center, University of Georgia, 315 Riverbend Road, Athens, Georgia, USA 30602 Backbone Resonance Assignments of Human Normal Adult Hemoglobin in the Deoxy Form: Sahu, S.C., Simplaceanu, V., Ho, N. T., Giovannelli, J. L. and Ho, C., Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA, USA The solution conformation of the type I hydrophobin EAS: J.P. Mackay1, A.H. Kwan1, J.M. Matthews1, R. Winefield2,3 and M. Templeton, 1University of Sydney, Sydney, Australia, 2Massey University, Palmerston North, New Zealand, 3Mt Albert Research Centre, Auckland, New Zealand Structural Determination of a High Potency Channel-Forming Peptides: Gabriel A. Cook1, Om Prakash1, Takeo Iwamoto1, Dejian Ma2, Bruce D. Schultz3, Yan Xu2, John M. Tomich1, 1 Biochemistry, Kansas State University, Manhattan, KS, USA, 2Anesthesia, University of Pittsburgh Medical School, Pittsburgh, PA, USA, 3Anatomy and Physiology, Kansas State University, Manhattan, KS, USA NMR studies of Cre recombinase: C. Amero, M. Foster, Biophysics Program, Ohio State University, Ohio, USA Structure and recognition of ubiquitination signals: Masahiro Shirakawa1,2, Kenichiro Fujiwara1, Ayako Ohno1,3, Takeshi Tenno1, JunGoo Jee1,2, Hidehito Tochio1, Hidekazu 1,3 1 2 Hiroaki , Yokohama City University, Kanagawa, Japan, RIKEN GSC, Kanagawa, Japan, 3 Kihara Memorial Yokohama Foundation for the advancement of Life Sciences, Kanagawa, Japan BIOPHYSICAL CHARECTERIZATION OF PROTEASE INDUCED ENZYMATIC DEGRADATION OF POLY-3-HYDROXY BUTRYIC ACID: Sumana Chatterjee, Department of Chemistry, Basanti Devi College, 147B, Rashbehari Avenue , Kolkata 700029, India NMR Investigations on Structure, Stability and pH Driven Monomer-Dimer transition in DLC8a: P. M. Krishna Mohan1, Amarnath Chatterjee1, Anindya Ghosh2, and Ramakrishna V. Hosur1, 1Department of Chemical Sciences, and 2Department of Biological Sciences, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai 400 005, India Functional dynamics at small and large time/size scales:Erik R.P. Zuiderweg. M. Revington, Y. Zhang, T.Wang, S.Cai, Biophysics, Biochemistry and Chemistry, The University of Michigan. 930 N. University Ave, Ann Arbor, MI 48109, USA Structural Plasticity of the Apoptosis Protein BAD: Rebecca S. Lipsitz, Richard J. Youle, and Nico Tjandra, Laboratory of Biophysical Chemistry, NHLIB,NIH Insights into the Formation of the Arsenate Reductase - Thioredoxin Complex: P. Vanhaesebrouck1, J. Messens2, K. Van Belle2, K. Wahni2, L. Wyns2, J. C. Martins1, 1NMR and Structure Analysis Unit, Universiteit Gent, Belgium, 2Department for Ultrastructure, Vrije Universiteit Brussel, Belgium Structure, Function and Stability of the HeadPiece C-terminal Domain: W. Vermeulen1, D. Bourry1, P. Vanhaesebrouck1, F. A. M. Borremans1, M. Van Troys2, C. Ampe2, J. C. Martins1, 1 NMR and Structure Analysis Unit and 2Department of Biochemistry, Universiteit Gent, Belgium Structure and recognition of ubiquitination signals: Masahiro Shirakawa1,2, Kenichiro Fujiwara1, Ayako Ohno1,3, Takeshi Tenno1, JunGoo Jee1,2, Hidehito Tochio1, Hidekazu Hiroaki1,3,

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Yokohama City University, Kanagawa, Japan, 2RIKEN GSC, Kanagawa, Japan, 3Kihara Memorial Yokohama Foundation for the advancement of Life Sciences, Kanagawa, Japan P150 Slow motion studies of a c-terminal complexed centrine by using cross correlated dynamics involving modulations of isotropic chemical shifts: Fatiha Kateb*, Luisa Poggi,* Daniel Abergel*, Gil Craescu $ and Geoffrey Bodenhausen*, *Ecole Normale Superieure, Paris; $Institut Curie, Orsay

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PROTEIN FOLDING P151 Implications of Molten Globule State(s) Involved in the Drug Delivery Process in Neocarzinostatin: S. Aranganathan1, 2, T. K. S. Kumar2, 3, Chin Yu2, 3 and Der-Hang Chin*1, 1 Departmnet of Chemistry, National Chung Hsing University, Taiwan, ROC, 2Department of Chemistry, National Tsing Hua University, Taiwan, ROC, 3Department of Chemistry and Biochemistry, University of Arkansas, USA NMR Investigation of Trp-Rich Helices: Mahalakshmi#, S. Raghothama* and P. Balaram#, Molecular Biophysics Unit# and Sophisticated Instruments Facility*,Indian Institute of Science, Bangalore 560012, India Expanding the Turn Segment of Designed -Hairpin Peptides: NMR Analysis: K. Muruga Poopathi Raja and P. Balaram, Molecular Biophysics Unit, Indian Institute of Science, Bangalore-560012 NMR Analysis of Designed -Hairpin Peptides with Modified -turn: K.Muruga Poopathi Raja and P.Balaram, Molecular Biophysics Unit, Indian Institute of Science, Bangalore-560012 Residual Dipolar Couplings from Denatured Proteins in Multiple Alignment Media: Erika Gebel1 and David Shortle, Department of Biological Chemistry, 1Program in Computational and Molecular Biophysics, The Johns Hopkins University School of Medicine, Maryland, USA Studies on the folding of proteins in solution as well as in membranes: Blake Hill, Guru Thuduppathy Probing the folding energy landscape of an EF-hand calcium binding protein through hydrogen exchange: Sulakshana Mukherjee, Kavita Kuchroo, Kandala V.R. Chary and Girjesh Govil, Department of Chemical Sciences, Tata Institute of Fundamental Research ,Homi Bhabha Road, Mumbai 400 005 India Protein Folding Kinetics by Relaxation Dispersion Measurements: Kaare Teilum1, Flemming M. Poulsen2 and Mikael Akke1, 1Department of Biophysical Chemistry, Lund University, Sweden, 2Department of Protein Chemistry, University of Copenhagen, Denmark Order amid disorder - Nascent structural motifs examined by residual dipolar couplings: K. Fredriksson,1 M. Louhivuori,2 A. Annila,2,3 1Program in Structural Biology and Biophysics Program, Institute of Biotechnology, 2Department of Physical Sciences, and 3 Department of Biosciences, University of Helsinki, Finland Interaction of DnaK Substrate Binding Domain with Apomyoglobin Polypetides: Implications for Protein Folding and Misfolding: Senapathy Rajagopalan, Nese Kurt, Carolina Vega, and Silvia Cavagnero*, Department of Chemistry, University of Wisconsin-Madison, 1101 University Ave., Madison, WI 53706, U.S.A. Protein Folding Studies of Marginally Stable Proteins by NMR Relaxation Methods : M. Tollinger,1 L.E. Kay,2 J.D. Forman-Kay,2 R. Konrat,11University of Vienna, Austria, 2 University of Toronto, Canada

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Studies of Residual Structure of Human Prion Protein hPrP (121-230): Jitendra Kumar, Christian Richter, Susanne Grimme and Harald Schwalbe, Johann Wolfgang Goethe-Universität, Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Marie Curie Strasse 11, D-60439, Frankfurt am Main, Germany NMR studies of Aromatic Interactions in Designed Peptides: R. Mahalakshmi#, S. Raghothama* and P. Balaram#, Molecular Biophysics Unit# and Sophisticated Instruments Facility*, Indian Institute of Science, Bangalore 560012, Indi

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PARAMAGNETIC PROTEINS P164 Correlation Between Hydrogen Bond Lengths and Reduction Potentials: Mutagenesis Studies on Residues 44 and 8 of Clostridium pasteurianum Rubredoxin : I-Jin Lin,1 Erika B. Gebel, 1,2 Timothy E. Machonkin, 1,3 William M. Westler, 1 and John L. Markley 1, 1 University of Wisconsin-Madison, Wisconsin, USA 2 Johns Hopkins University, Maryland, USA 3 University of Rochester, New York, USA

MEMBRANE PROTEINS P165 Conformational study of the membrane-spanning fusogenic peptides using solid-state NMR : Prashant Agrawal1, Frans Hulsbergen1, Mathias Hofmann2, Dieter Langosch2, Nico Meeuwenoord3, Hermen Overkleeft3 and Huub de Groot1, 1 Biophysical Organic Chemistry, Leiden Institute of Chemistry, Leiden University P.O. box 9502, 2300 RA, Leiden, The Netherlands, 2 Lehrstuhl Chemie der Biopolymere, TU München, Weihenstephaner Berg 3, 85354 Freising-Weihenstephan, Germany , 3 Bio-organic Synthesis, Leiden Institute of Chemistry, Leiden University P.O. box 9502, 2300 RA, Leiden, The Netherlands Solution NMR structural studies of MBP: M.M.Monette2, D.S. Libich1, V.J. Roberston1, G.Harauz1, 1University of Guelph, Guelph, Ontario, Canada; 2Bruker BioSpin, Milton, Ontario, Canada Measurement of residual dipolar couplings for integral membrane proteins and structure refinement of OmpA in DPC micelles: Tomasz Cierpicki, Binyong Liang, Lukas Tamm and John H. Bushweller, Department of Molecular Physiology and Biological Physics, University of Virginia Solution structure of TF1Fo ATP synthase subunit c : T. Nakano 1, T. Ikegami 1, T. Suzuki 2, 3, M. Yoshida 2, 3, H. Akutsu 1, 1Osaka University, Osaka, Japan, 2Tokyo Institute of Technology, Kanagawa, Japan, 3Japan Science and Technology Corporation, Kanagawa, Japan Solid-State NMR Studies of the Membrane Interactions of A42 from Alzheimer's Disease: Crystal T.L. Lau1, Kevin J. Barnham2, Colin L. Masters2 and F. Separovic1, 1School of Chemistry and 2Department of Pathology, The University of Melbourne and 2The Mental Health and Research Institute, VIC 3010, Australia Is membrane interaction domain a necessity for localization: Phospholipase C delta1 as an example of shuttling protein? Srinivas N. Pentyala, Departments of Anesthesiology, Urology, Physiology & Biophysics, School of Medicine, State University of New York, Stony Brook, NY, USA Proton-decoupled 15N solid-state NMR investigation of synthetic ion-channel peptide reconstituted in oriented lipid bilayers: Sudheendra U.S and Burkhard Bechinger, FRE 2446, University Louis Pasteur, 4, rue Blaise Pascal, 67000 Strasbourg, FRANCE

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Structural Changes associated with Mycobacterium tuberculosis H37Rv ESAT-6:CFP-10 omplex Formation: Akshaya Kumar Meher*, Naresh Chandra Bal*, Kandala V. R. Chary,$ and Ashish Arora*, *Molecular and Structural Biology, Central Drug Research Institute, Lucknow 226

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001, India, and $Department of Chemical Science, Tata Institute of Fundamental Research, Mumbai 400 004, India NUCLEIC ACIDS STRUCTURE P173 Structure-Function Analysis of Picornaviral Internal Cis-acting RNA Replication Elements:Varatharasa Thiviyanathan, Yan Yang, Rene Rijnbrand, Kumar Kaluarachchi, Stanley M. Lemon, and David G. Gorenstein, Sealy Center for Structural Biology, University of Texas Medical Branch, Galveston, Texas 77555, USA Structural Roles of CTG Repeats in DNA Trinucleotide Repeat Expansion: L.M. Chi and S.L. Lam, Department of Chemistry, The Chinese University of Hong Kong, Hong Kong Unusual Dynamics of A·A Mismatch with 5’-Purine and 3’-Pyrimidine Flanking Bases: C. W. Kwok and S. L. Lam, Department of Chemistry, The Chinese University of Hong Kong, Hong Kong Structural and thermodynamic investigation of the HIV-1 frameshift inducing element: David W. Staple and Samuel E. Butcher, Department of Biochemistry, University of Wisconsin-Madison Structure of stem-loop d from a key picornaviral replication site: H. Huang,*2 S.J. Headey,*1 J.K. Claridge,1 G.A. Soares,1 K. Dutta,3 D. Yang,4 Pascal, S.M.1, 1Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand, 2Department of Biochemistry & Biophysics, University of Rochester Medical Center (present address: Vaccinex Incorporated, Rochester NY), 3New York Structural Biology Center, New York, NY, 4Department of Biological Sciences & Department of Chemistry, National University of Singapore

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OLIGOSACCHARIDES AND PROTEINS P178 NMR Studies of C-linked Carbo--amino acids Containing Variety of Sugar Moieties, K. Narsimulu, K. V. S. Ramakrishna, A. Ravisankar, K. Ravinder Reddy, V. Subhash, P. Nagender, B. Srinivas, P. Jayaprakash, Palakodety Radha Krishna, B. Jagannadh, G. V. M. Sharma and A. C. Kunwar, Indian Institute of Chemical Technology, Hyderabad, India-500 007 Identification of Ligand Fragments and their Binding Orientation Using WaterLOGSY and 1D Selective Inter-ligand QUIET-NOEs: B. J. Stockman, D. T. A. Hadden, P. V. Sahasrabudhe, J. T. Herberg, J. C. Hagadorn, J. P. Martin Jr., D. C. Rohrer, Pfizer, Inc., Pfizer Global Research & Development, Groton, Connecticut, USA Dissection study and inhibitor design targeting SARS 3C-like protease: Jiahai Shi and Jianxing Song , Department of Biological Sciences, National University of Singapore, 10 Kent Ridge Crescent, Singapore 119260 Identification of novel inhibitors of the ZipA/FtsZ complex by NMR: Désirée H. H. Tsaoa, Yuanhong Lia, Thomas S. Rush IIIa, Lidia Mosyaka, Mark Stahl, Karl Malakian, Lee D. Jenningsb, Alan G. Sutherlandb, Alexey Ruzind and Juan Alvareza, Wyeth Research, 87 Cambridge Park Drive, Cambridge, MA 02140, Chemical and Screening Sciences, Structural Biology and Computational Chemistrya, Medicinal Chemistryb and Infectious diseasesc Tracking Apo-Necocarzinostain Conformational Changes that may Corresponds to Chromophore Release Using NMR Analysis at Residue Level : Christopher G. Sudhahar1, Der-Hang Chin1*, 1Department of Chemistry, National Chung Hsing University, Taichung, Taiwan, ROC NMR Based Investigations of Drug Induced Phospholipidosis From Early Prediction to Marker Assessment: Kris A. Borzilleri1, Jinghai J. Xu1, Margaret C. Dunn1, Markus Boehm1, Lora Robosky2, Michael Reily2, David Baker2, Anne Tilloy-Ellul3, Marie-Therese Masson3, Bishop Wlodecki1, Keith C. Jendza1, Michael A. Brodney1, Linda A. Chatman1, Susan D.Anway1

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and Jane M. Withka1, Pfizer Global Research and Development – Arbor, MI, 3 Amboise, France P184 Study on the complexation between DNA Takako Ohyama1,Hajime Mita1 and Yasuhiko Yamamoto1, applied sciences, University of Tsukuba, Tsukuba, JAPAN
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Can structural features explain differences in potency between the Ga and Y Complexes of DOTATOC? M. V. Deshmukh 1, G. Voll 1, A. Kühlewein 1, H. Mäcke 2, J. Schmitt 2, H. Kessler 1 1 , Gerd Gemmecker 1, Chemistry Department, TU Munich, Garching, Germany, 2 Institute of Nuclear Medicine, University Hospital, Basel, Switzerland Structure Assisted Alteration of AT-Recognition Profile: A Study of Drug-DNA Complex: Prateek Pandya and Surat Kumar, Applied Sciences, Faculty of Engineering, Dayalbagh Educational Institute, Dayalbagh, Agra-282 005 Solution conformation of Substance P antagonists, [D-Arg1, D-Trp7,9, Leu11]-SP, [DArg1, D- Pro2, D-Trp7,9, Leu11]-SP and [D-Pro2, D-Trp7,9]-SP by CD, NMR and MD Simulations: Arati Prabhua, Alpeshkumar Maldea, Sudha Srivastavab and Evans Coutinhoa*, a Department of Pharmaceutical Chemistry, Bombay College of Pharmacy, Kalina, Mumbai 400 098, India, bTata Institute of Fundamental Research, Homi Bhabha Road, Navy Nagar, Colaba, Mumbai 400 005, India Probing the effect of N- and C- terminal length on the conserved G-P-GR segment in the V3 loop of HIV-1: *Sudha Srivastava, #Meena Kanyalkar, *Mamata Joshi, @Evans Coutinho and @$Anil Saran, *National Facility for High Field NMR, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai -400005, India, # $ P.K.M.K. College of Pharmacy, Worli, Mumbai –400018, India, CSIR @ Emeritus Scientist, Department of Pharmaceutical Chemistry, Bombay College of Pharmacy, Kalina, Santacruz, Mumbai -400098 Correlation between binding cooperativity and protein conformational flexibility as studied by hydrogen-to-deuterium amide NH exchange: Vladimir I. Polshakov1,2, Berry Birdsall3, Thomas A. Frenkiel4 and James Feeney3, 1 Center for Drug Chemistry, Moscow, Russia, 2 Research Center for Magnetic Tomography & Spectroscopy, M.V. Lomonosov Moscow State University, Moscow, Russia, 3 National Institute for Medical Research (NIMR), London, 4 United Kingdom, MRC Biomedical NMR Centre, NIMR, London, United Kingdom
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C NMR Relaxation Studies Reveal a Complex Pattern of Motion in the Binding Site for Human U1A Protein: Z.Shajani1 and G.Varani1,2, Department of Chemistry1 and Department of Biochemistry2 Design, Synthesis and Characterization of a Novel Cyclic Curcumin-cystine Bioconjugate with their antifungal and antioxidant properties: Neha kapoor & Krishna misra*, Centre for Biotechnology, University of Allahabad, Allahabad - (211002) The Binding Site of Acetylcholine Receptor From Synthetic Peptides to Mimitope Structure: T. Scherf,1 R. Kasher2, M. Balass,2 M. Fridkin, 3 S. Fuchs,4 and E. Katchalski-Katzir2 , Departments of 1Chemical Research Support, 2Biological Chemistry, 3Organic Chemistry and 4 Immunology, Weizmann Institute of Science, Rehovot 76100, Israel Phage Library for Molecular Recognition Analysis by NMR: H. Takahashi1, Y. Mizukoshi2, M. Nagasu2, and I. Shimada1, 3, 1BIRC, AIST, Tokyo, Japan, 2JBIRC, JBIC, Tokyo, Japan, 3The University of Tokyo, Tokyo, Japan NMR study of homo and hetero oligomers of furanoid based sugar amino acid: S. Kiran Kumar, Saumya Roy, T. K. Chakraborty and A. C. Kunwar, Indian Institute of Chemical Technology, Hyderabad, India 500 007

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Application of DOSY in Identification of Peptide Conformers in Solution: B. Kumaran1, Rajkishor Rai2, S. Raghothama1, 1Sophisticated Instruments Facility, 2Molecular Biophysics Unit, Indian Institute of Science, Bangalore – 560 012 Laccase Catalyzed Cross-linking of Peptides and Proteins: M.-L. Mattinen,1 C. L. 2 1 1 1 2 1 1 Steffensen, K. Kruus, R. Lantto, K. Autio, J. H. Nielsen, J. Buchert , VTT Biotechnology, Espoo, Finland, 2DIAS Research Centre Foulum, Tjele, Denmark Structure of adriamycin complexed with d-TGATCA by Proton and Phosphorus-31 Nuclear Magnetic Resonance Spectroscopy : P. Agrawal,1 S. K. Barthwal,2 and R. Barthwal1, Department of Biotechnology1 and Physics2, Indian Institute of Technology Roorkee, 247667, India H and 31P NMR studies on binding of anticancer drug mitoxantrone with d-CGATCG: M. Kaur1, P. Awasthi1, Monica1, S.K. Barthwal2 and R. Barthwal1, Department of Biotechnology1 and Physics2, Indian Institute of Technology Roorkee, 247667, India Determination of 13C CSA tensor parameters: Extension of the model-independent approach to an RNA kissing complex undergoing anisotropic rotational diffusion in solution: Sapna Ravindranathan1, Chul-Hyun Kim2, Geoffrey Bodenhausen3, 1National Chemical Laboratory, Pune, India, 2California State University, Hayward CA, USA, 3Ecole Normale Supérieure, Paris, France and Ecole Polytechnique Fédérale, Lausanne, Switzerland EPR IMAGES OF CHROMIUM (V) IN PADDY (Oryza Sativa) ROOTS: K. VICTOR BABU and T. RAMASAMI, Chemical Physics Department, Central Leather Research Institute- Council of Scientific and Industrial Research, Adyar, Chennai – 600 020, India Structure of antitumor agent mitoxantrone wth DNA hexamer d-(ATCGAT)2 by 1H and 31P NMR: R. Durairaj1, Prashansa Agrawal1, S. K. Barthwal 2, Ritu Barthwa11, Department of Biotechnology1 and Physics2, Indian Institute of Technology Roorkee, Roorkee 247 667, India NMR based solution structure of antitumor drugs, Berberine and Palmatine: Lata Chauhan1, Kushuma Bisht1, Sudhir Kumar Barthwal2 And Ritu Barthwal1, Dept. Biotechnology1 And Physics2, Indian Institute Of Technology Roorkee, 247667, India NMR based solution structure of anticancer drugs, Sanguinarine and Luteolin: Santosh Kumari1, Amit Kumar1, S.K. Barthwal2 and Ritu Barthwal1, Dept. Biotechnology1 and Physics2, Indian Institute of Technology, Roorkee, 247 667, India
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MR IN HUMAN HEALTH & BEHAVIOUR, IN VIVO SPECTROOSCOPY, METABONOMICS P204 Phosphorus MR spectroscopic changes mediated by choline kinase knock-down in a human breast tumor model: K. Glunde1, N. Mori1, V. Raman1, and Z. M. Bhujwalla1, 1Johns Hopkins University School of Medicine, Baltimore, Maryland, United States Determination of cholesterol in human serum and bile using Proton Nuclear Magnetic Resonance spectroscopy: Y. Jadegoud1, Madhulika Srivastava1, G. A. Nagana Gowda1, V. Ramesh2, Pratul Sinha3, Ajay Sharma4, V. K. Kapoor4 and C. L. Khetrapal1, 1Centre of Biomedical Magnetic Resonance, Departments of 2Pathology, 3Transfusion Medicine and 4Surgical Gastroenterology, Sanjay Gandhi Post Graduate Institute of Medical Sciences, Raebareli Road, Lucknow 226 014, INDIA Quantification of glycine and taurine conjugated bile acids in human bile using 1H NMR spectroscopy: Omkar Ijare1, B. S. Somashekar1, G. A. Nagana Gowda1, V. K. Kapoor2 and C. L. Khetrapal1, 1Centre of Biomedical Magnetic Resonance and 2Department of Surgical Gastroenterology, Sanjay Gandhi Post-graduate Institute of Medical Sciences, Raebareli Road, Lucknow-226 014, INDIA

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Prediction of therapeutic outcome in patients with Fulminant Hepatic Failure using 1H Nuclear Magnetic Resonance spectroscopy: Varsha Saxena1, Ashish Gupta1, G.A. Nagana Gowda1, Rajan Saxena2, S. K. Yachha3 and C. L. Khetrapal1, 1Centre of Biomedical Magnetic Resonance, Departments of 2Surgical Gastroenterology and 3Gastroenterology, Sanjay Gandhi Post Graduate Institute of Medical Sciences, Raebareli Road, Lucknow 226 014, INDIA
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H NMR spectroscopy for the diagnosis of urinary tract infection with special reference to Pseudomonas aeruginosa and Klebsiella pneumonia: Ashish Gupta1, Mayank Dwivedi2, G. A. Nagana Gowda1, Archana, Ayyagari2, A. A. Mahdi3, M. Bhandari4 and C. L. Khetrapal1, 1 2 Centre of Biomedical Magnetic Resonance and Departments of Microbiology and 4 Urology, Sanjay Gandhi Postgraduate Institute of Medical Sciences, 3Department of Biochemistry, KGMU Lucknow
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H NMR study of Malabsorption Syndrome: Lakshmi Bala1, Uday C. Ghoshal2, Ujjala Ghoshal3, G. A. Nagana Gowda1 and C. L. Khetrapal1, 1Centre of Biomedical Magnetic Resonance and Departments of 2Gastroenterology and 3Microbiology Sanjay Gandhi Post Graduate Institute of Medical Sciences, Raebareli Road, Lucknow- 226 014, India Age Related Differences in the BOLD Post-Stimulus Undershoot: K. Gopinath1, C. Wierenga2,3, T. Conway2,3, B. Crosson2,3, R. Briggs1, 1Department of Radiology, University of Texas Southwestern Medical Center, Dallas, TX, USA, 2Department of Clinical Psychology, University of Florida and 3VA Brain Rehabilitation R & D Center, Gainesville, FL, U.S.A. Web Accessible MR decision support system for brain tumour diagnosis and prognosis, incorporating in vivo and ex vivo genomic and metabolomic data (FP6-2002LIFESCIHEALTH 503094); Acronym: eTUMOUR, Bernardo Celda Lexical processing in trilingual subjects: cortical mapping using fMRI: S.S. Kumaran,Y. Uma Sreekumar, S. Khushu and R.P. Tripathi, NMR Research Centre, Institute of Nuclear Medicine and Allied Sciences, Brig. S.K. Mazumdar Road, Delhi – 110 054, INDIA Role of Diffusion weighted imaging and MR spectroscopy in Radiation necrosis: Ashok Kumar, Shilpi Modi, S.S. Kumaran, S. Khushu, Prabhjot Kaur and R.P. Tripathi, NMR Research Centre, Institute of Nuclear Medicine and Allied Sciences, Brig. S.K. Mazumdar Road, Delhi – 110 054, INDIA Volumetric MRI analysis of the Hippocampus with aging: S Khushu, S Sharma, S S Kumaran, R P Tripathi, NMR Research Centre, Institute of Nuclear Medicine and Allied Sciences, Lucknow Road, Delhi 110054, India In-vivo Measurement of Apparent diffusion coefficient in normal and malignant prostate tissue: Virendra Kumar*, R. Kumar#, S. Thulkar@, S. Duttagupta$, A.K. Hemal#, N.P. Gupta# and N.R. Jagannathan* , Departments of NMR*, Urology# , Radiodiagnosis@ and Pathology$, All India Institute of Medical Sciences, New Delhi – 110029. INDIA Differentiation of Abdominal Body Fluids by In Vitro 1-H MR Spectroscopy for Clinical Applications: Sang Soo Shin, Heoung Keun Kang, Gwang Woo Jeong, Department of Radiology, Chonnam National University Medical School, Kwangju 501-757, Korea NMR Analysis of Biological Fluids in Epilepsy Associated with anti-GAD Antibodies: U. C. Marx1, G. D. Jackson2,3, D. J. Craik1, L. Kinton2, S. F. Berkovic2,3, R. M. Wellard2 , 1Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia, 2Brain Research Institute, Melbourne, VIC 3081, Australia, 3Department of Medicine, University of Melbourne, VIC 3081, Australia Determination of brain metabolite concentrations by in vivo localized proton spectroscopy with correction of relaxation effect: Nashiely PINEDA ALONSO *, Serge AKOKA **, Evelyne BAGUET **, Frederique TOULGOAT *, Hubert DESAL *, * Service de Neuroradiologie Diagnostique et Interventionnelle. Hospital G&R Laennec. CHU de Nantes, France, **

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Laboratoire d'Analyse Isotopique et Electrochimique de Metabolisme. UMR CNRS 6006, University of Nantes. France P219 Quantitative identification of the protonation state of histidines in vitro and in vivo: N. Shimba,1,2 Z. Serber,1 C.S. Craik,1 V. Dötsch1, 1University of California San Francisco, USA, 2 Ajinomoto Co., Japan The Origin of T2 in Articular Cartilage MRI as a Function of its Maturation: Hadassah Shinar, Keren Keinan-Adamsky, Gil Navon, School of Chemistry, Tel Aviv University, Tel Aviv 69978, Israel A Technique for the Measurement of Renal ATP in a Large Animal Model of Septic Shock : R. M. Wellard1, G. Pell1, J. Williams2, C. May2, L. Wan2, G. D. Jackson1,3, R. Bellomo4 , 1Brain Research Institute, Melbourne, Australia, 2University of Melbourne, Howard Florey Institute, 3 Department of Medicine, University of Melbourne, 4Intensive Care, Austin Health, Melbourne, Australia Cerebral Pyruvate Carboxylase Flux is Unaltered during Intense Activation: Anant B. Patel1, Golam M.I. Chowdhury2, Robin A. de Graaf1, Douglas L. Rothman1, Robert G. Shulman1, Kevin L. Behar2, Department of 1Diagnostic Radiology and 2Psychiatry, Magnetic Resonance Research Center, Yale University School of Medicine, New Haven, CT 06520, USA In-vivo Proton MRS of Brain in Chronic Obstructive Pulmonary Disease Patients: Virendra Kumar*, S. Sinha@, R. Guleria@, U. Sharma* and N. R. Jagannathan*, Departments of NMR* and Medicine@, All India Institute of Medical Sciences, New Delhi – 110 029, India Application of Spectral Deconvolution Method for Evaluation of Brain Tumors: in vivo 1-H MR Spectroscopy: HK Kang, GW Jeong, JJ Seo, HJ Kim, Department of Radiology, Chonnam National University Medical School, Gwangju 501-190, Korea Potential of various in vivo MR methodologies in the evaluation of cancer: Virendra Kumar, Uma Sharma, KA Danishad and NR Jagannathan, Department of NMR, All India Institute of Medical Sciences, New Delhi. India Utility of Proton Magnetic Resonance Spectroscopic Imaging (MRSI) in Breast Danishad KA*, Kumar V*, Sharma U*, Seenu V#, Jagannathan NR*, Departments of and Surgery#, All India Institute of Medical Sciences, New Delhi -110029, INDIA Cancer: NMR*

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Proton MR CSF Analysis and New Software as Predictors for the Differentiation of Meningitis in Children, a Subramanian A., b Gupta A., b Saxena S., c Gupta A., d Kumar R., e Nigam A., e Kumar R., f Mandal S.K. and a Roy R, a NMR Laboratory, Division of SAIF, Central Drug Research Institute, Lucknow, India, (rajaroy_cdri@yahoo.com) b Babu Banarasi Das National Institute of Technology and Management, Lucknow, India, c Center for Biomedical Magnetic Resonance and d Department of Pediatric Neurosurgery, Sanjay Gandhi Post-Graduate Institute of Medical Sciences, Lucknow, India, e Department of Paediatrics, King George’s Medical University, Lucknow, India, f Division of Biometry and Statistics, Central Drug Research Institute, Lucknow, India Proton NMR Analysis and Identification of Predictive Metabolite-Descriptors for the Differentiation of Unresponsive and Responsive Strains in Leishmania donovani: a,‡ Subramanian A., b Srivastava M., c Roy U., c Rastogi A.K., b Mandal S.K. and a Roy R, a NMR Laboratory, Division of SAIF, Central Drug Research Institute, Lucknow, India, (rajaroy_cdri@yahoo.com) b Division of Biometry and Statistics, Central Drug Research Institute, Lucknow, Indi,. cDivision of Biochemistry, Central Drug Research Institute, Lucknow, India, ‡ Practice School Division, Birla Institute of Technology & Science, Pilani, Rajasthan, India Cholesterol Esters and Ceramide in Human Intracranial Tuberculomas: a Subramanian A., b Joshi B.S. and a Roy R, a NMR Laboratory, Division of SAIF, Central Drug Research Institute, Lucknow, India, (rajaroy_cdri@yahoo.com), b Bruker India Scientific Pvt. Ltd., Lucknow, India

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NMR Spectroscopic Evaluation of Axillary Nodes in Breast Cancer:U. Sharma*, M.N. Pavan Kumar@, V. Seenu@ and N. R. Jagannathan*, Departments of NMR*and Surgery@, All India Institute of Medical Sciences, New Delhi – 110029, India Detailed molecular differentiation among gliomas by HR-MAS. A precise classification of GBM.: MC.Martínez-Bisbal, D. Monleón, V. Esteve, MB. Martínez-Granados and B. Celda, Depto. Química Física, Universitat de Valencia, c/Dr. Moliner, 50, 46100-Burjassot (Valencia) Spain Anti-inflammatory Treatment Reduced Breast Cancer Cell Invasion and Caused Metabolic Changes Characteristic of a Less Malignant Phenotype:, B. Gimi, D. Artemov, Z.M. Bhujwalla, Radiology - MR Research, Johns Hopkins University, Baltimore, MD, USA VEGF Overexpression Increased Invasion and Altered Metabolism in a Human Prostate Cancer Cell Line Co-cultured with Endothelial Cells under Hypoxia: F. Wildes, V. Raman, D. Artemov, and Z.M. Bhujwalla, Radiology, JHU ICMIC Program, Johns Hopkins University, Baltimore, MD, USA Development of uniformly 13C, 15N-labeling methods in animal system for a hetero-nuclear NMR-based metabolomics: Michitaka Suto1, Takashi Nishihara1 & Jun Kikuchi1,2,3, 1Grad. Sch. Integ. Sci., Yokohama City Univ; 2GSC, RIKEN Yokohama Inst. & 3CREST, JST The hetero-nuclear NMR-based metabolomics reveals incorporation of 13C, 15N-compounds into higher plants: Kenji Akamine1, Takashi Hirayama1,2,3 and Jun Kikuchi1,2,4, 1Grad. Sch. Integ. Sci., Yokohama City Univ; 2GSC, RIKEN Yokohama Inst.; 3Plant Mol. Biol. Lab., RIKEN Tsukuba Inst. and 4CREST, JST Effect of oxygen level on metabolic fluxes and metabolite levels of yeast studied by NMR spectroscopy: Paula Jouhten, Minna Perälä, Eija Rintala, Laura Ruohonen, Merja Penttilä and Hannu Maaheimo, VTT Technical Research Centre of Finland, Helsinki, Finland Induction of in vitro metabolism and motility in asthenospermic human spermatozoa by Larginine and nitric oxide synthesis: associated with active sperm anion transport system: Sudha Srivastava, #Anita Agarwal, Rahul Jaiswal and Girjesh Govil, National Facility for High Field NMR, Tata Institute of Fundamental Research, Homi Bhabha Road, Mumbai –400005, India #Department of Physiology, Seth G. S. Medical College,Parel, Mumbai-400006, India

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ESR P238 Measurement of oxygen and superoxide in the perfused heart by EPR spectroscopy: Vijay Kumar Kutala, Mark G Angelos, Carlos A Torres, Jason D Stoner, Marwan Mohammad, Periannan Kuppusamy, Davis Heart Lung Research Institute, Ohio State University, Columbus, OH,USA MRI Study of Root Hair Dynamics and Micro Scale Water Uptake Patterns: T. Kushnir1, E. Segal2, Y. Itzchak1 and U. Shani2, 1Department of Diagnostic Imaging, MRI Unit, The Chaim Sheba Medical Center, Tel Hashomer, Israel, 2Department of Soil & Water Sciences, Faculty of Agricultural, Food and Environmental Quality Sciences, Hebrew University of Jerusalem, Rehovot, Israel MRI shows intravenous and intra amygdala Kainic Acid increase rat CBF: M. T. Acosta, J. P. Munasinghe, M. Banerjee, A.Yamaguchi, M. A. Rogawski, M. Angstadt, T. Wilson, A. Silva, W. Theodore, A. Koretsky, National Institute of Neurological Disease and Stroke, National Institute of Health, Bethesda, Maryland, United States

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COMPUTATIONAL METHODS

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Early Prediction of White Matter Changes in Tumor Cases due to Radiotherapy using Magnetic Resonance Images: S.B.MEHTA ,1 S.CHAUDHURY,2 A. BHATTACHARYYA ,3 A. JENA4, 1S. B. Mehta, Delhi College of Engineering Bawana road, Delhi – 110 042. 2(Prof. ) Dr. S. CHAUDHURY Indian Institute of Technology Hauz khas, Delhi – 110 016. 3(Prof.) Dr. A. BHATTACHARYYA, Delhi College of Engineering Bawana road, Delhi – 110 042, 4 Dr. A. Jena Chief MRI, MRI Center, Rajiv Gandhi Cancer Hospital, Rohini, Delhi 110085 Simulations of chemical exchange in NMR using QSim: Magnus Helgstrand, Dept. of Biophysical Chemistry, Lund University, SE-221 00 Lund, Sweden Experimental demonstration of Complementarity of Entanglement and Interference by Nuclear Magnetic Resonance:Arindam Ghosh and Anil Kumar , NMR Quantum Computation and Quantum Information Group Department of Physics and Sophisticated Instruments Facility, Indian Institute of Science, Bangalore-560012, India Nuclear Magnetic Resonance implementation of adiabatic Deutsch-Jozsa algorithm: Avik Mitra, Arindam Ghosh, Ranabir Das and Anil Kumar, NMR Quantum Computation and Quantum Information Group Department of Physics and Sophisticated Instruments Facility, Indian Institute of Science, Bangalore-560012, India Programmable quantum state discriminator by Nuclear Magnetic Resonance: T. Gopinath, Ranabir Das, and Anil Kumar, NMR Quantum Computing and Quantum Information Group, Department of Physics and Sophisticated Instruments Facility, Indian Institute of Science, Bangalore-560012, India Automated Structure Determination of Proteins from NMR data: W. Gronwald, J. Trenner, K. Brunner, B. Ganslmeier, A. Nassar, R. Kirchhöfer, K.-P. Neidig and H. R. Kalbitzer, Institute of Biophysics and Physical Biochemistry, University of Regensburg, 93040 Regensburg, Germany and Bruker Biospin, Rheinstetten, Germany The use of unassigned signals in NMR structure determination: Eiso AB1, David Pugh,2 Rob Kaptein,1 Rolf Boelens,1 and Alexandre Bonvin1, 1University of Utrecht, The Netherlands. 2 University of the Western Cape, South Africa SolARIA: automated cross-peak assignment for MAS solid-state NMRIn the last years, solid- state NMR developed towards a technique suitable for solving structures of immobilised proteins at atomic resolution.: Fossi Michele, Department of NMRSupported Structural Biology, Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert- Rössle-Str. 10, 13125 Berlin, Germany Calculations of Chemical Shielding and Electric Field Gradient Tensors in Molecular Sieves: Gurpreet Singha, S. Ganapathya , J. P. Amoureuxb ,J. F. Paulc and S. Cristolc, aNMR Facility, National Chemical Laboratory, Pune, India, bLCPS, University of Sciences and Technologies, Lille, cLaboratoire Catalyse, University of Sciences and Technologies, Lille THEORETICAL MODEL OF ACTIN, R.Sagajkar, Accelrys Software Solution AORTIC SMOOTH MUSCLE -1LVT:

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INFORMATICS, EDUCATION AND CAPACITY BUILDING P251 The New York Structural Biology Center, NMR Facility: Michael Goger, JeanChristophe Hus, Boris Itin, Kaushik Dutta & David Cowburn, NMR Facility, NYSBC, 89 Convent Avenue, New York, New York, 10027-7556, USA NMR FEATURES IN THE NEW RCSB PROTEIN DATA BANK QUERY ENGINE: Gary L. Gilliland1 and who from SDSC2Ken Addess2, Nita Desphande2 and Helen Berman1, RCSB

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Protein Data Bank: 1Rutgers, the State University of New Jersey, Department of Chemistry, Piscataway, NJ 08854, 2San Diego Supercomputer Center at the University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093 P253 A new approach for determining the orientation of a weakly bound ligand in the receptor binding pocket. The epothilone-A / Tubulin complex: V.M. Sánchez,1 M. Reese,1 J. Meiler,2 M.J. Blommers,3 C. Griesinger,1 T. Carlomagno1, 1 Max Planck Institute for Biophysical Chemistry, Goettingen, Germany, 2 University of Washington, Seattle, USA, 3 Core Technologies, Novartis Pharma AG, Basel, Switzerland. Solution structure of RNA containing GU bulge: NMR study of r (CUGGGCGG). r (CCGCCUGG): R. P. Ojha, Biophysics Unit, Department of Physics, DDU Gorakhpur University, Gorakhpur – 273 009, India Solution conformation two peptides derived from bovine seminalplasmin (SPLN) protein by 1 H NMR and restrained molecular dynamics:P. N. Sunil Kumar1, C. Sadasivan1, K. S. Devaky2 and M. Haridas1*, 1Department of Life Sciences, Kannur University, Palayadu, Kerala-670 661, India, 2School of Chemical Sciences, Mahatma Gandhi University, Kottayam, Kerala-686 560, India. Helical Formation and Conformational Stability in Homo and Hetero Oligomoers of Furanoid cis--Sugar-Amino Acid: B. Jagadeesh, A. Prabhakar, S. Chandrasekhar, M.S. Reddy and B. Jagannadh, Indian Institute of Chemical Technology, Tarnaka, Hyderabad- 500 007, India.

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NATIONAL MAGNETIC RESONANCE ABSTRACTS P257 Chemical shift evolution based separation of the integrals of partially resolved doublets using non-selective RF pulses G. A. Nagana Gowda, Centre of Biomedical Magnetic Resonance, Sanjay Gandhi Post graduate Institute of Medical Sciences, Raebareli Road, Lucknow, 226 014, INDIA A new class of thermotropic-lyotropic liquid crystals: An NMR study: S. Somashekar1, G.A. Nagana Gowda1, Hui Chen2 and David Abdallah2, R.G. Weiss2 and C.L. Khetrapal1, 1Centre of Biomedical Magnetic Resonance, Sanjay Gandhi Post Graduate Institute of Medical Sciences, Lucknow, India, 2 Department of Chemistry, Georgetown University, Washington D.C., USA A Novel Intramolecular Rearrangement Investigated by NMR Leading to the Synthesis of Biheterocyclic Indole-Benzoimidazole derivatives on Solid Phase: aRoy A.D., b Kundu B. and a Roy R. a NMR Laboratory, Division of SAIF, Central Drug Research Institute, Lucknow, India. (rajaroy_cdri@yahoo.com) b Division of Medicinal and Process Chemistry, Central Drug Research Institute, Lucknow, India. Studies on Catalytic Behavior of FCC Catalysts by 29Si and 27 Al MAS NMR Techniques: Babita Behera, Siddharth Ray, I.D.Singh, Indian Institute of Petroleum, Dehradun-248005 Aminoquinazolines to Imidazoquinazolines: Mechanism of Cyclisation via Structure Elucidation Leading to Transamidation in Solid Phase: a,¶ Grover R.K., a Sharma S., b Kundu B. and a Roy R., a NMR Laboratory, Division of SAIF, Central Drug Research Institute, Lucknow, India. (rajaroy_cdri@yahoo.com) b Division of Medicinal and Process Chemistry, Central Drug Research Institute, Lucknow, India. ¶ Present Address: Department of Chemistry, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA. Preparation and relaxation studies of Fe2O3 conjugated with biologically compatible polymers: Rashi Mathur, Rakesh Kumar Sharma, Anil Kumar Mishra*, Institute of Nuclear Medicine and Allied Sciences, Brig. SK Mazumdar Road, Delhi-110054, India, akmishra@inmas.org

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