Document Sample


                         AND POSTER SESSION

                     On Interactions Between Biomolecules

Poster location:
              Hall Went gebouw, Sorbonnelaan 16,             Wednesday, April 25th, 2001
              De Uithof, Utrecht                             Thursday, April 26th, 2001

Symposium location:
            Auditorium of the Hogeschool van Utrecht,
            Padualaan 101, Utrecht
            Limited adjacent parking

                                  7th Bijvoet Tutorial Symposium 2001

                        POSTER PRESENTATION

This seventh tutorial symposium builds on the format of the preceding ones. The
symposium will be accompanied by a poster session in which the research activities of
the Bijvoet Graduate School for Biomolecular Chemistry are presented. The posters
will be constantly on Wednesday afternoon, April 25th 2001. This poster session will
be attended in part by members of the Scientific Advisory Board of the School. The
board will judge all posters with respect to scientific merit and quality of presentation.
The best poster will be awarded with a prize on Thursday afternoon.

The symposium and the poster program are devoted to various aspects of the structure,
function and interaction of biomolecules. The two-day meeting is intended for
everybody interested in structural biology. All Ph.D. students, postdoctoral fellows
and staff members working at the Bijvoet Graduate School are expected to actively
participate in this event. It creates unique possibilities to become fully aware of the
multi-disciplinary approach that is necessary to solve problems related to the
functioning of biomolecules.

A focal point of the research activities of the Bijvoet Graduate School for
Biomolecular Chemistry is the study of molecular structure, dynamics, recognition
and interaction. Modern molecular biological methods, enzymic and/or chemical
synthesis, and separation techniques are applied to obtain molecules and molecular
complexes. These molecules are chosen with a view towards their function in
biological processes. To study the compounds and their complexes with
complementary molecules, sophisticated instrumental and biological techniques are
used. Advanced nuclear magnetic resonance spectroscopy, mass spectrometry, X-ray
diffraction, interaction analysis, isotope labelling, and computational techniques are
applied to gain insight into the fundamental aspects of molecular recognition.

I hope that this meeting will be successful and that it will be an inspiration for new
collaborative efforts to tackle challenging problems in the field of bioactive molecules.

Prof.dr. Rob Kaptein, Research Director
Bijvoet Graduate School for Biomolecular Chemistry

The sponsoring of the lecture of
Prof.dr. Axel Brunger by Akzo Nobel (Organon), Oss, is gratefully acknowledged.

                                 7th Bijvoet Tutorial Symposium 2001

PROGRAM for APRIL 25th 2001
14.00 h       Registration and mounting of posters (Hall Went gebouw)

14.15 h           Poster session

16.30 h           Closure of poster session

                              PROGRAM for APRIL 26th 2001
 8.30 h      Coffee and Registration, hand-out of Abstracts

 9.00 h      Prof.dr. Rob Kaptein

 9.10 h      Prof.dr. Paul A. Bartlett, University of California at Berkeley, Berkeley, CA, USA
                   “Peptidomimetics and Proteomimetics”

10.00 h      Prof.dr. Hagan Bayley, Texas A&M University, College Station, TX, USA
                   “Interior design of a transmembrane pore”

10.50 h           Coffee and Tea break

11.20 h      Prof.dr. Axel T. Brunger, Stanford University, Stanford, CA, USA
                   “Structural studies of Ca2+-dependent synaptic vesicle fusion”
                                                                               (Organon Lecture)

12.10 h      Prof.dr. Stephan Grzesiek, University of Basel, Basel, Switzerland
                   “Spectroscopy of hydrogen bonds and other technical developments in high
                   resolution NMR”

13.00 h           Lunch

14.00 h      Prof.dr. Ari Helenius, ETH, Zurich, Switzerland
                   “Why Glycoproteins contain glycans”

14.50 h      Prof.dr. Gerald W. Hart, John Hopkins University, Baltimore, MD, USA
                   “Dynamic glycosylation of Nuclear and cytosolic proteins: A challenge to
                   proteomics and functional analysis of signal transduction and

15.40 h      Prof.dr. David L. Smith, University of Nebraska-Lincoln, Lincoln, NE, USA
                   “Exploring the folded structures of proteins by hydrogen exchange/mass

16.30 h      Poster Award
16.45 h      Closure
17.00 h             Mixer with drinks and refreshments

                                    7th Bijvoet Tutorial Symposium 2001

                                               Peptidomimetics and Proteomimetics"

                                                                Paul A. Bartlett

                      Department of Chemistry, University of California, Berkeley, CA 94720-1460, USA

             α-H elix tem p lates:
                  O       O O                      H3N+                               H3N+         N+
                                                                N                                 N
                                                                H NH                              H NH
                      N               CO2¯                       OC                                OC

             "@-Tid es" as β-sheet tem p lates:
                              O                    O
              O                                                     H                         N       O¯
                          N                    N                    N                N            N
                N                   N                    N                       HN H O           H O
                H O                 H O                  H O
                                                                                 OC O H           O H
                O H                 O H                  O H
                                                                                   N   N        N   N
              N   N               N   N                N   N
                                                                                              O H     O
              H                                                     O                 HO
                              O                    O
Our understanding of intra- and intermolecular interactions in biological systems can be greatly
enhanced by the synthesis and evaluation of analogs and mimics of the naturally occurring molecules
involved. We have designed scaffolds that orient hydrogen-bonding moieties in the same way as
found in well-defined elements of protein secondary structure. These molecules template α-helical
or β-sheet conformations in appended peptides and thus serve as 'proteomimetics'.

    R1                        R1                               R1
         O                            O                             O            As the outgrowth of projects in combinatorial
                      RCON                         RCON
O    N       R2                   N       R2                    N        R2      synthetic design, we have developed
                                                                                 heterocyclic templates based on amino acid
     N O                          N O                      O    N        O       subunits that can serve as novel, rigid β-turn
     R3                           R3                                             mimics.
                                                       O                R3

                                                        7th Bijvoet Tutorial Symposium 2001

                               Interior design of a transmembrane pore

                                               Hagan Bayley
 Department of Medical Biochemistry & Genetics, The Texas A&M University System Health Science Center, College
                                              Station, Texas, USA

My laboratory is using genetic engineering and targeted chemical modification to produce
functionalized pore-forming proteins. The primary target of our studies has been staphylococcal α-
hemolysin, which is a 293 amino-acid, water-soluble polypeptide that self assembles in lipid bilayers
to form heptameric transmembrane pores. Recently, we have concentrated on making radical
modifications to the lumen of the α-hemolysin pore. First, non-covalent adapters such as
cyclodextrins have been used to change the pore's conductance, ion selectivity and susceptibility to
blockers (1;2). Second, the covalent attachment of polymers has allowed us to study polymer motion
and to produce pores that interact with and respond to other macromolecules (3). Engineered protein
pores may have applications in biotechnology, for example, for the controlled permeabilization of
cells (4) and as components of biosensors (3;5)

                                               Reference List

   1. Gu, L.-Q.; Braha, O.; Conlan, S.; Cheley, S.and Bayley, H.(1999) Stochastic sensing of
      organic analytes by a pore-forming protein containing a molecular adapter. Nature 398, 686-
   2. Gu, L.-Q.; Dalla Serra, M.; Vincent, J.B.; Vigh, G.; Cheley, S.; Braha, O.and Bayley,
      H.(2000) Reversal of charge selectivity in transmembrane protein pores by using non-
      covalent molecular adapters. Proc.Natl.Acad.Sci.USA 97, 3959-3964
   3. Movileanu, L.; Howorka, S.; Braha, O.and Bayley, H.(2000) Detecting protein analytes that
      modulate transmembrane movement of a polymer chain within a single protein pore. Nature
      Biotechnology 18, 1091-1095
   4. Eroglu, A.; Russo, M.J.; Bieganski, R.; Fowler, A.; Cheley, S.; Bayley, H.and Toner,
      M.(2000) Intracellular trehalose improves the survival of cryopreserved mammalian cells.
      Nature Biotechnology 18, 163-167
   5. Bayley, H.; Braha, O.and Gu, L.-Q.(2000) Stochastic sensing with protein pores. Adv.Mater.
      12, 139-142

                                        7th Bijvoet Tutorial Symposium 2001

                                                                                        Organon Lecture

                   Structural studies of Ca2+-dependent synaptic vesicle fusion

                                              Axel T. Brunger
       Department of Molecular & Cellular Physiology, Stanford University, Stanford, CA, 94305-5489, USA

Synaptic transmission is the major means by which neurons communicate with one another in the
nervous system. The pre- and postsynaptic events are highly regulated and subject to stimulated
changes that modulate the releasable pool and the release-probability of synaptic vesicles. Thus, this
"synaptic plasticity" could play a role in learning. The molecular components involved in
neurotransmission interact in a hierarchical fashion: some components have mutual pair-wise
interactions, some components have interactions that are restricted to adjacent partners, and some
components or groups of components are spatially separated by compartments. In addition, some of
the interactions are sequential. This complexity allows the neuron to create multiple regulatory
mechanisms for neuronal plasticity. Structural studies are presented about some of the complexes
between the individual molecular components. This information will then provide the framework for
investigations that are targeted at the dynamical aspects of the system. Understanding the molecular
machinery that controls and regulates synaptic neurotransmission will be important for knowledge-
based therapeutics to treat neurological disorders.

                                        7th Bijvoet Tutorial Symposium 2001

  Spectroscopy of hydrogen bonds and other technical developments in high resolution NMR

                  Stephan Grzesiek, M. Barfield, F. Cordier, A. Dingley, J. Feigon,
                         L. K. Nicholson, V.Jaravine, H.J. Sass, G Musco.
                Biozentrum, University of Basel, Klingelbergstr. 70, CH-4056 Basel, Switzerland

Direct evidence for the existence of individual hydrogen bonds in biomacromolecules has been
provided by the detection of trans-hydrogen bond scalar couplings in RNA, DNA, proteins, and their
complexes. These scalar couplings are electron-mediated and can be used to identify the three
partners involved in the hydrogen bond, i.e. the donor, the acceptor and the proton. The size of the
trans-hydrogen bond scalar couplings correlates with the strength of the hydrogen bond and with the
chemical shift of the proton involved in the H-bond. We will show applications to a number of
different folded and unfolded biomacromolecules, explore the possibility to obtain further insights
into macromolecular structures from the quantitation of the H-bond couplings, and discuss the
correlation of the size of the couplings with other NMR parameters. As a second topic, I will discuss
the possibility to obtain high resolution spectra of biomacromolecules within polyacrylamide gels. I
will also describe the diffusional properties within such phases and the possibility to obtain weak
alignment either by mechanical stress or embeeding of other substances. The results of the residual
dipolar coupling measurements under these conditions are then used for structure refinement by a
new algorithm that obviates the explicit input of the components of the orientation tensor.

                                        7th Bijvoet Tutorial Symposium 2001

                                  Why Glycoproteins contain glycans

                                                Ari Helenius
                Institute of Biochemistry, Universitaetstr. 16, ETH, Zurich, CH-8092, Switzerland

N-linked oligosaccharides arise when blocks of fourteen sugars are added co-translationally to newly
synthesized polypeptides in the endoplasmic reticulum (ER). The glycans are then subjected to
extensive modification as the glycoproteins mature and move through the ER via the Golgi complex
to their final destinations inside and outside the cell. In the ER, where the repertoire of
oligosaccharide structures is still rather small, the glycans play a pivotal role in folding,
oligomerization, quality control, sorting, and transport of newly synthesized glycoproteins. They are
used by the cells as universal ‘tags’ that allow specific lectins and modifying enzymes to establish
order among the diversity of maturing glycoproteins. Calreticulin (CRT) and calnexin (CNX), two
homologous lectin-like chaperones that interact specifically with glycoproteins that carry
monoglucosylated trimming intermediates of the N-linked glycans, belong to the most important of
the ER chaperones. As part of a complex cycle, they are involved in folding, quality control and ER
associated degradation of glycoproteins. To characterize CRT and CNX function in more detail we
analyzed the structure of the conserved P-domain of CRT. The data revealed a unique, elongated,
finger-like domain in which the repetitive nature of the sequence is maintained at the 3D structure
level. The function of the domain is being analyzed in further studies. We also investigated the
molecular basis of quality control by analyzing the substrate specificity of the major folding sensor,
the lumenal UDP-glucose:glycoprotein glucosyltransferase (GT), a key factor in the CNX/CRT
cycle. It determines when glycoproteins are folded and ready to be exported to the Golgi complex.
When their role in folding is completed, N-linked glycans acquire more complex structures and a
new set of functions. The division of synthesis and processing between the ER and the Golgi
complex represents an evolutionary adaptation that allows efficient exploitation of potential of

                                         7th Bijvoet Tutorial Symposium 2001

                     Dynamic Glycosylation of Nuclear and Cytosolic Proteins:
                        A Challenge to Proteomic and Functional Analyses
                          of Signal Transduction and Phosphoregulation.

        Gerald W. Hart, Yuan Gao, Lance Wells, Frank I. Comer, Sai Iyer, Natasha Zachara,
                         Keith Vosseller, Zhiyu Li, and Kazuo Kamemura
 Department of Biological Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, MD
                           21205-2185; Fax: (410) 614-8804; email:

Our laboratory continues to elucidate the functions of the dynamic glycosylation of nuclear and
cytoskeletal proteins by O-linked N-acetylglucosamine (O-GlcNAc). O-GlcNAc is an abundant
protein modification that is as dynamic and as abundant as protein phosphorylation in all
multicellular eukaryotes and many viruses. Current data suggests that O-GlcNAc levels on proteins
are highly responsive to glucose metabolism, perhaps providing a mechanism for ‘switching-off’
phosphorylation sites on some proteins. Indirect data suggests that abnormal O-GlcNAc modification
plays a role in diabetes, Alzheimer’s disease, transcriptional regulation and many other cellular
processes. We have developed proteomic methods for the identification and site mapping of O-
GlcNAc modified proteins in which state-of-the-art mass spectrometry plays a key role.

Some Other Recent Highlights: 1) The O-GlcNAc Transferase (OGT) tightly associates with
phosphatases, consistent with its proposed ‘yin-yang’ relationship to O-phosphorylation on some
proteins. 2) The gene for an O-GlcNAcase from human brain has been cloned and characterized. 3)
The major O-GlcNAc site (Ser16) on the estrogen receptor ß (ER-ß) is reciprocally phosphorylated.
Modification at this O-GlcNAc/O-phosphate site regulates ER-ß transcriptional activity, as well as
its turnover rate. 4) Yeast two-hybrid analyses have identified many proteins that interact with the
tetratricopeptide (TPR) repeat domain of the O-GlcNAc Transferase, regulating its myriad of
intermolecular associations. 5) Most of the basal transcription factors, including RNA polymerase II
and the TATA-binding protein, are multiply O-GlcNAcylated. In vitro, phosphorylation of the CTD
of RNA polymerase prevents its glycosylation and vice versa. 6) SR RNA splicing proteins are
reciprocally O-GlcNAcylated/O-phosphorylated. The glyco-SR proteins are localized to the
cytoplasm and the phosphoforms are localized to the nucleus. One major glyco-SR protein associates
with ribosomes and appears to play a role in RNA export. 7) Knock-out studies of OGT, in
collaboration with the Marth group at UCSD, have shown that OGT is an X-linked gene, and that O-
GlcNAc is required for life at the level of a single cell. 8) OGT activity and selectivity are exquisitely
regulated by its multimerization (mediated by the TPR domains), by its post-translational
modification, and by the UDP-GlcNAc/UDP levels in the cell throughout a large concentration range
(micromolar to millimolar). 9) Facile mass spectrometric methods for mapping sites of O-
GlcNAcylation/ phosphorylation have been developed and applied to synaptic vesicle regulatory
proteins. 8) Insulin promoter factor –1 (IPF-1), the glucose-sensitive transcription factor regulating
insulin synthesis, and PPAR-γ, a nuclear receptor important to insulin signalling are both multiply O-
GlcNAcylated. 10) The retinoblastoma, Rb proteins are reciprocally O-GlcNAcylated/O-
phosphorylated, suggesting a role for O-GlcNAc in the cell cycle.

Taking an eclectic approach, involving much method development, we hope to elucidate the roles of
the dynamic O-GlcNAc modification of nuclear and cytosolic proteins and to evaluate the
relationship between O-phosphate and O-GlcNAc. Supported by NIH Grants HD13563, CA42486, a
grant from the Juvenile Diabetes Fdn, and a grant from American Health Assistance Fdn.

                                          7th Bijvoet Tutorial Symposium 2001

     Exploring the folded structures of proteins by hydrogen exchange/mass spectrometry

                                             David L. Smith
                      Department of Chemistry and Eppley Institute for Cancer Research
                              University of Nebraska Lincoln, NE 68588, USA

Hydrogens located at peptide amide linkages in unfolded polypeptides are rapidly replaced with
deuterium when the polypeptides are incubated in D20. However, hydrogens in the same
polypeptides, but folded, exchange very slowly. This structure- induced reduction in hydrogen
exchange rates, which may be as large as 108, is attributed primarily to intramolecular hydrogen
bonding and reduced access to the solvent. Thus exchange in a-helices and P-sheets is usually slow,
as is exchange in the hydrophobic cores of large proteins. Exchange in poorly formed loop regions
on the surfaces of proteins is often rapid. In addition, binding of ligands may shield hydrogens
located within binding sites from exchange. The utility of hydrogen exchange as a probe of the
folded structures of proteins has been recognized for nearly 50 years. Several methods, including
radioactivity, infrared and UV absorbance spectroscopies, and nuclear magnetic resonance have been
used to detect hydrogen exchange. Recent advances in mass spectrometry have facilitated its use for
detecting hydrogen exchange in proteins. This presentation will focus on the fundamental
considerations required to design experiments using hydrogen exchange/mass spectrometry, and will
include several recent applications of this method in studies of protein folding and ligation.

                                       7th Bijvoet Tutorial Symposium 2001

                        Poster presentation on Wednesday 25th 2001
Biochemistry of Membranes
Ingrid Vereijken          Fructans insert between the headgroups of phospholipids

Eric Strandberg              The snorkeling behavior of side chains in model transmembrane peptides is dependent on the lipid
                             headgroup composition

Bio-organic Chemistry
Minke Noordermeer:           Cloning and characterization of fatty acid hydroperoxide lyase; a biocatalyst for the production of food
                             Minke A. Noordermeer, Gerrit A. Veldink and Johannes F.G. Vliegenthart

Mario van der Stelt          Anandamide, a lipid with cannabinoid activity, protects rat brain against in vivo neuronal injury
                             Mario van der Stelt, Wouter Veldhuis, Gijs van Haaften, Dop Bär, Gerrit Veldink, Vincenzo Di Marzo,
                             Hans Vliegenthart and Klaas Nicolay

Bertrand Kleizen             FLAG epitope interferes with the biosynthesis of D F508-CFTR in semi-permeabilized cells

Annemieke Jansens            Non-native disulfide bonds form during LDL receptor folding
                             Annemieke Jansens and Esther van Duyn

Sean Austin                  Host-dependent glycosylation of a recombinant glycoprotein
                             S. Austin, K. Koles, P. van Berkel, L. van Buuren, J.P. Kamerling and J.F.G. Vliegenthart

Christian Grün               Isolation and characterisation of alpha-(1-3)-glucan from model yeast Schizosaccharomyces pombe
                             Christian H. Grün, Frans Hochstenbach, Frans M. Klis, Johannis P. Kamerling, Johannes F.G.

Dirk Lefeber                 Neoglycoconjugate vaccines of synthetic Streptococcus pneumoniae type 3 oligosaccharides coupled to
                             Dirk J. Lefeber, Barry Benaissa-Trouw, Kees Kraaijeveld, Harm Snippe, Simon Haseley, Johannis P.
                             Kamerling, and Johannes F.G. Vliegenthart

Vincent van Miegem           Saturation transfer difference NMR experiment applied to the interaction between alpha-hCG and its
                             glycan at position Asn78
                             Vincent van Miegem, Paul J. A. Erbel, Johannis P. Kamerling & Johannes F. G. Vliegenthart

Eelco van Anken              Not all disulphides bonds of HIV Envelope are essential for proper folding and infectivity
                             Eelco van Anken, Maarten de Kok, Rogier Sanders, Martijn Dankers, Kati Holopainen, Ben Berkhout
                             & Ineke Braakman

Biomolecular Mass Spectrometry
Ewald van den Bremer      Folding of the enzymatic domain of the DNase colicin E9 studied by mass spectrometry
                          Ewald van den Bremer a, Claudia S. Maier a, Colin Kleanthous b & Albert J. R. Heck a
                           Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences
                            School of Biological Sciences, University of East Anglia, UK

Pauline Bonnici              Competitive Binding Studies of Vancomycin-group Antibiotics and Nisin to Lipid II
                             Pauline J. Bonnici a, Eefjan Breukink b, Kees Versluis a & Albert J. R. Heck a
                              Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences
                               Department of Biochemistry of Biomembranes, Bijvoet Center and Institute of Biomembranes

Edwin Romijn                 Proteomics screen for ER resident folding factors
                             Edwin P. Romijn a*, Eelco van Anken b*, Claudia Maggioni b*, Roberto Sitia c, Ineke Braakman b &
                             Albert J.R. Heck a * contributed equally to this work
                              Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences
                               Dept Bio-organic Chemistry, Bijvoet Center
                               Laboratory of Molecular Immunology DIBIT-HSR, Milano Italy

Jeroen Demmers               Investigation of protein-biomembrane interactions by nanoESI-MS.
                             Jeroen A.A. Demmers a,b, J. Antoinette Killian b & Albert J. R. Heck a
                             Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences

                                               7th Bijvoet Tutorial Symposium 2001

                                   Department of Biochemistry of Biomembranes, Bijvoet Center and Institute of Biomembranes

Martijn Pinkse                 Mass spectrometric analysis of autophosphorylation and cyclic nucleotide binding of the cGMP
                               dependent protein kinase Iα from bovine lung.
                               Martijn W. H. Pinkse a, Claudia S. Maier a, Klaus Rumpel b & and Albert J. R. Heck a
                                Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences
                                 Pfizer Global Research and Development, Sandwich, UK

F. Tempels                     Determination of Binding Constants of Vancomycin-Group Antibiotics using Affinity Capillary
                               F.W.A Tempels a, P.J.Bonnici a, and A. J. R. Heck a
                                Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences

Nora Tahallah                  Cofactor-dependent assembly of the flavoprotein vanillyl-alcohol oxidase
                               Nora Tahallah a, Claudia S. Maier a, Robert H. H. van den Heuvel b; Willem J. H. van Berkel b &
                               Albert J. R. Heck a
                                Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences
                                 Dept. Biomolecular Sciences, Laboratory of Biochemistry, Wageningen University

J. J. Kettenes-van den Bosch   Metal Binding Selectivity of Modified Cyclic Peptides Isolated from the Ascidian Lissoclinum Patella
                               J. J. Kettenes-van den Bosch a, C. Versluis a, A.J.R. Heck a, L.A. Morris b, B.F. Milneb & M. Jaspars b
                                Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences
                                 Marine Natural Products Laboratory, Department of Chemistry, University of Aberdeen, Scotland,

Anne Kleinnijenhuis            Localization of intramolecular monosulfide bridges in Nisin with bond selective tandem mass
                               A.J. Kleinnijenhuis a, A.J.R. Heck a, R.M.A. Heeren b and M.C. Duursma b
                                Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences
                                 FOM Institute AMOLF, Amsterdam

M. Isabel Catalina             Mass spectrometric studies of tandem and single SH2 domains of Syk kinase.
                               M. Isabel Catalina a, Claudia S. Maier a, Richard C. Blom b, Frank A. Redegeld b & Albert J. R. Heck a
                                Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences
                                 Dept. Pharmacology & Pathophysiology, Utrecht Institute for Pharmaceutical Sciences

Y. Surroca                     Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin by
                               MALDI-MS after extraction from SDS-PAGE
                               Y. Surroca a, J. Haverkamp a & A. J. R. Heck a
                                Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences

Jeroen Krijgsveld              Identification by Mass Spectrometry of the Drosophila Chromatin Remodeling Complex, Brahma
                               Jeroen Krijgsveld a #, Arnoud J. Kal b #, Peter Verrijzer b # & Albert J. R. Heck a #
                                Dept Biomolecular Mass Spectrometry, Bijvoet Center and Utrecht Inst. for Pharmaceutical Sciences
                                 Department of Molecular and Cell Biology,Leiden University Medical Center
                                 a joint effort through the Center for Biomedical Genetics

Crystal and Structural Chemistry
Sjors Scheres:             Conditional Dynamics and its potential use in the macromolecular phase problem.
                           S.H.W. Scheres and P. Gros

Stan Konings                   Development of a peptide vaccine against Meningitis MD-simulation of peptides based on VR-family
                               P1.16 of PorA Neisseria Meningitis
                               Stan Konings, Clasien Oomen, Alexandre Bonvin*, Piet Gros

Bogos Agianian                 The high resolution crystal structure of the Drosophila Sigma GST: a beginning to understanding its
                               role in the flight muscles

Eric Huizinga                  Crystal structure of the von Willebrand Factor A1 domain in complex with botrocetin

Clasien Oomen                  From protein structure to peptide vaccine design of subtype-specific vaccines for Neisseria

                                                   7th Bijvoet Tutorial Symposium 2001

A. Schouten              Crystal structure of mouse phosphatidylinositol transfer protein (PITPα) without bound
                         A. Schouten, B. Agianian, J. Westerman, J. Kroon, K.W.A. Wirtz, P. Gros

A. Schouten              Crystal structure of two-chain botrocetin, a vWF modulator from the venom bothrops jararaca
                         A. Schouten, E.G. Huizinga, J.J. Sixma, J. Kron, P. Gros

Lucy Vandeputte-Rutten   Crystal Structure of the outer membrane protease OmpT from Escherichia coli reveals a novel catalytic

Medicinal Chemistry
Frank Dekker             Binding of short peptide ligands to the lck SH2 domain, a study on flexibility
                         F.J. Dekker, N.J. de Mol, H.W. Hilbers, J. Kemmink, R.M.J. Liskamp

B.Wels                   Synthesis of novel torn mimetics incorporating peptidomimetic residues

Christopher J. Arnusch   Combinatorial and structure-based modifications of the Vancomycin antibiotic core structure

I. Vrasidas              Multivalent carbohydrae ligands based on dendrimers

Jeroen van Ameijde       Sugar corks for porin

Reshma Autar             Towards multivalent carbohydrates that block bacterial adhesion and infection

A. J. Brouwer            Convergent synthesis and diversity of amino acid based dendrimers

Dr. S.B.A. Halkes        Gallic acid inhibits the interaction between hemoglobin and vegetable tannins

NMR Spectroscopy
Henry Jonker:            Protein-protein interaction in transcriptional activation; NMR Study of the PC4-VP16 complex
                         Henry Jonker, Gert Folkers, Rainer Wechselberger, Rolf Boelens en Rob Kaptein

Alexandre Bonvin:        The NMR structure of Chymotrypsin Inhibitor 2 from chemical shifts and cross hydrogen-bonds J-
                         couplings: How far can we get?
                         A.M.J.J. Bonvin, K. Houben, M. Guenneugues, R. Kaptein and R. Boelens.

Alexandre Bonvin:        Hydration structure and Dynamics of a collagen peptide: a combined NMR and molecular dynamics
                         A.M.J.J. Bonvin, G. Melacini, M. Goodman, R. Boelens and R. Kaptein

Nocky Derix              Probing the nature of the signalling state of Photoactive Yellow Protein by NMR: Hydrogen/Deuterium
                         exchange data and pH dependence
                         Nocky M. Derix, C. Jeremy Craven, Klaas J. Hellingwerf, Rolf Boelens and Rob Kaptein

                                           7th Bijvoet Tutorial Symposium 2001

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