Molten Globule State of Globular Proteins

Abstract

A molten globule state has been assumed to be a major intermediate of protein folding. The conformational stability of the acidic molten globule state of several proteins and the corresponding state of a synthetic model polypeptide is determined by the balance of the electrostatic repulsive forces, which favor the extended unfolded state, and the opposing forces mainly hydrophobic interactions, which favor the compact molten globule state.