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 occurs only in the core of proteins.
D)Trapped water stabilizes the helix and sheet structures.

Question

Quizplus · Accepted Answer

The core of proteins is typically hydrophobic, meaning it avoids interactions with water. The polar N-H and C=O moieties of the peptide backbone can disrupt this hydrophobic core, so they are neutralized by forming hydrogen bonds between themselves within α-helix and β-sheets structures. This helps to stabilize the protein's structure and keep the hydrophobic core intact.

Why Should the Core of Most Globular and Membrane Proteins