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Biochemistry

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Biochemistry





Proteins

Learning Objectives

By the end of this lesson you will be able to explain that:

 The elements which make up proteins are carbon,

hydrogen, oxygen, nitrogen (plus a few others).

 Amino acids are the monomers of which proteins are

composed.

 The condensation of amino acids leads to the

formation of dipeptides, polypeptides and proteins.

 Hydrolysis of proteins reverses this process

 The primary, secondary and tertiary structures of

proteins gives them their properties

 relationship of structure to function in fibrous and

globular proteins.

A diverse group of biochemicals

 structure e.g. collagen (bone, cartilage, tendon), keratin (hair), actin

(muscle)

 enzymes e.g. amylase, pepsin, catalase, etc (>10,000 others)

 transport e.g. haemoglobin (oxygen), transferrin (iron)

 pumps e.g. Na+K+ pump in cell membranes

 motors e.g. myosin (muscle), kinesin (cilia)

 hormones e.g. insulin, glucagon

 receptors e.g. rhodopsin (light receptor in retina)

 antibodies e.g. immunoglobulins

 storage e.g. albumins in eggs and blood, caesin in milk

 blood clotting e.g. thrombin, fibrin

 lubrication e.g. glycoproteins in synovial fluid

 toxins e.g. diphtheria toxin

 antifreeze e.g. glycoproteins in arctic flea

 and many more!

Structure

Functional group









Amino group

Carboxyl group



 R-group give the amino acid its properties.

 Can contain S

dipeptides

 The formation of a dipeptide results from the

condensation reaction between two amino

acids.



H2O

Dipeptides





peptide bridge









N-terminus

C-terminus

Polypeptides

 Several amino acids linked together!

 Polypeptides that fold up and have a 3-D

structure are called proteins

 4 structures to be aware of…

Primary Structure

 This is just the sequence of the amino acids

in the chain.

Secondary Structure

 Alpha Helix









 Beta sheets

Tertiary structure

 The 3-D structure

 Every protein has a unique 3-

D structure

 Arises from:

 hydrogen bonds, which are

weak.

 ionic bonds between R-

groups with positive or

negative charges, which are

quite strong.

 sulphur bridges - covalent S-S

bonds between two cysteine

amino acids, which are

strong.

Sulphur bridge

Quaternary Structure

 This is only found in

proteins consisting of

more than one

polypeptide chain.

Globular and fibrous proteins

 Most proteins are globular

 Some are fibrous

 Some have regions of both!

Independent study

 Compare the structures and functions of

globular and fibrous proteins.

Biochemical tests



Biuret test for protein

grind up sample

add Biuret solution

lilac colour indicates protein

present



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