In general molecular chaperone proteins function by
A)mediating disulfide bond formation
B)synthesizing new proteins when one is misfolded.
C)preventing premature folding by binding hydrophobic regions of the protein.
D)enhancing salt bridge formation.
E)none of the above

Question

Quizplus · Accepted Answer

Molecular chaperone proteins prevent premature folding by binding to the hydrophobic regions of the protein. This can prevent misfolding, aggregation, and degradation of the protein, allowing it to properly fold into its functional conformation. Molecular chaperones do not mediate disulfide bond formation, synthesize new proteins, or enhance salt bridge formation.

In General Molecular Chaperone Proteins Function by