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.

Question

Quizplus · Accepted Answer

The highly polar N−H and C=O moieties of the peptide backbone must be neutralized in the hydrophobic core of the protein to avoid unfavorable interactions with the aqueous environment. The α-helix and β-sheet structures provide a way for the polar backbone to be neutralized while still allowing for hydrogen bonding within the protein.

Why Should the Core of Most Globular and Membrane Proteins