Multiple Choice
Why should the core of most globular and membrane proteins consist almost entirely of α-helix and β-sheets?
A) Hydrogen bonded structures must be kept away from water solvent.
B) Highly polar N−H and C=O moieties of the peptide backbone must be neutralized in the hydrophobic core of the protein.
C) Hydrogen bonding only occurs in the core of proteins.
D) Trapped water stabilizes the helix and sheet structures.
E) None are true.
Correct Answer:

Verified
Correct Answer:
Verified
Q10: Arrange the steps involved in folding of
Q11: Fibrous proteins contain polypeptide chains _ producing
Q12: In the tertiary structure of a protein,
Q13: _ between tightly packed amino acid side
Q14: Tertiary structure is defined as:<br>A) the sequence
Q16: All of the statements about the tertiary
Q17: The amino acid residue most likely to
Q18: _ are examples of antiparallel α-helix proteins.<br>A)
Q19: _ are proteins that help other proteins
Q20: _ amino acids are almost never found