Protein folding and function Flashcards
1
Q
Give 4 key features of a-helix secondary structures
A
- 3.6 amino acids per turn
- 0.54nm pitch
- Right-handed helix
- Carboxyl group is bonded to the NH group 4 amino acids away via hydrogen bonds
2
Q
Which two amino acids are strong helix formers?
A
Alanine and leucine
3
Q
B-pleated sheets exist in which two conformations?
A
Parallel and anti-parallel
4
Q
Give an example of a fibrous protein.
A
Collagen
5
Q
What are the roles of globular proteins?
A
Catalysis and regulation
6
Q
Describe the structure of amyloid fibres
A
Lots of B sheet, misfolded and insoluble, stabilised by hydrophobic interactions. A core B sheet forms before the rest of the protein
7
Q
What is a protein’s secondary structure?
A
Its local spatial arrangement of the polypeptide backbone
