1- Protein Structure

Question 1

GAPVIL

Answer 1

Non polar side chains:
Glycine
Alanine
Proline 
Valine
Isoleucine
Leucine

Question 2

CAsTTS

Answer 2

Polar side chains:
Cysteine
Asparagine 
Tyrosine
Threonine
Serine

Question 3

Positive side chains (al)

Answer 3

Lysine, arginine

Question 4

Negative side chains (ag)

Answer 4

Aspartate, glutamate

Question 5

What form are protein amino acids in?

Answer 5

L form

Question 6

What are the bonds in an alpha helix?

Answer 6

hydrogen bonds between the C=O of one residue and N H of another four amino acids along the helix stabilise the structure

Question 7

What are the bonds in a beta pleated sheet ?

Answer 7

hydrogen bonds between C=O and N H of different residues of two or more β strands holds the sheet together

Question 8

Why does proline cause a kink in the alpha helix

Answer 8

Proline causes kinks in the helix, because the N H group of the amino acid chain is lost, causing a kink to appear in the helix

Question 9

Give an example of a protein which is modified post- translationally

Answer 9

γ carboxyglutamate is formed from glutamate, this is used in several clotting cascade proteins by increasing calcium binding

Question 10

How does warfarin work

Answer 10

The anticoagulant WARFARIN works by inhibiting the carboxylation reaction, so reducing the
coagulative properties of the clotting factors
( less γ carboxyglutamate formed)