Direct evidence for a dry molten globule intermediate during the unfolding of a small protein.

ABSTRACT: Little is known about how proteins begin to unfold. In particular, how and when water molecules penetrate into the protein interior during unfolding, thereby enabling the dissolution of specific structure, is poorly understood. The hypothesis that the native state expands initially into a dry molten globule, in which tight packing interactions are broken, but whose hydrophobic core has not expanded sufficiently to be able to absorb water molecules, has very little experimental support. Here, we report our analysis of the earliest observable events during the unfolding of single chain monellin (MNEI), a small plant protein. Far- and near-UV circular dichroism measurements of GdnHCl-induced unfolding indicate that a molten globule intermediate forms initially, before the major slow unfolding

SUBMITTER: Jha SK 

PROVIDER: S-EPMC2718347 | biostudies-literature | 2009 Jul

REPOSITORIES: biostudies-literature