FFLD 6

Question 1

Super-secondary structure refers to:
A. Large alpha-helices and beta-sheets
B. The final fold of a protein
C. The close association of more than one piece of secondary structure into a functional unit
D. The association of more than one polypeptide chain in a functional protein

Answer 1

C

Question 2

All of the information required for the correct folding of a protein is in the:
A. Primary structure 
B. Secondary structure
C. Tertiary structure
D. Quaternary structure

Answer 2

A

Question 3

Which one of the following statements about chaperone proteins is correct?
A. They bind to other proteins and permanently prevent them from folding
B. All proteins require chaperone proteins to fold correctly as the amino acids need instructions about what bonds to form with which amino acids
C. They facilitate correct protein folding through hydrophobic interactions by preventing incorrect protein folding
D. There is only one type of chaperone protein and it required ATP to function

Answer 3

C

Question 4

The key finding from Afinsen’s experiment on protein folding was:
A. That proteins can be denatured with chemicals
B. That proteins can fold when denaturing conditions are removed
C. That disulphide bonds can form under oxidising conditions
D. That the only information required for proteins to fold correctly is the sequence of amino acids (primary structure)

Answer 4

D

Question 5

What types of non-covalent bonds are involved in stabilising the protein structure, i.e. holds the protein together, stopping it from falling apart once it’s been folded up? (Select all that are correct)
A. Hydrophobic interactions
B. Hydrogen bonds
C. Electrostatic interactions/ionic bonds
D. Metal ion coordination
E. Disulphide bonds

Answer 5

A, B, C and D