Folding Intermediate in the Villin Headpiece Domain Arises from Disruption of a N-Terminal Hydrogen-Bonded Network

摘要

A complete understanding of protein folding requires knowledge of the structure and energetics of various states on the free energy landscape and of how specific interactions, as well as environmental effects, modulate their relative stabilities and the mechanism for interconversion. In a traditional view, small globular proteins are thought to fold cooperatively in which only the native (folded) and denatured (unfolded) states are populated at equilibrium. Advances in NMR techniques have allowed direct measurement of transiently and sparsely populated intermediates for small fast-folding proteins under native conditions, thus providing evidence for a more complex picture of protein folding.