Within the native tertiary structure of a typical globular protein, interactions between an alpha-helix and a beta_sheet would occur primarily
A) after the incorporation of a prosthetic group during polypeptide folding.
B) by non-covalent interactions among the amino acid side chains.
C) following the hydrolysis of ATP.
D) in the presence of one or more chaperones.
E) near the ends of these structural conformations.

Question

Quizplus · Accepted Answer

The interactions between an alpha-helix and a beta-sheet within the native tertiary structure of a typical globular protein would occur primarily through non-covalent interactions among the amino acid side chains. These interactions would be stabilizing and essential for the overall stability and function of the protein. Prosthetic groups or chaperones are not necessarily involved in these interactions, and hydrolysis of ATP is unlikely to be directly related to alpha-helix/beta-sheet interactions. The location of these interactions would not be limited to the ends of the structures.

Within the Native Tertiary Structure of a Typical Globular Protein