In allosteric regulation,effector molecules usually bind

Question

Quizplus · Accepted Answer

Allosteric regulation involves a reversible change in the shape of a protein due to the binding of an effector molecule to an allosteric site, which is a site on the protein that is distinct from the active site. The binding of the effector molecule is noncovalent, meaning that there is no formation of a chemical bond between the protein and the effector molecule. Therefore, the best choice is C, which describes the reversible and noncovalent binding of effector molecules during allosteric regulation.

In Allosteric Regulation,effector Molecules Usually Bind