Experimental evidence for a frustrated energy landscape in a three-helix-bundle protein family.

ABSTRACT: Energy landscape theory is a powerful tool for understanding the structure and dynamics of complex molecular systems, in particular biological macromolecules. The primary sequence of a protein defines its free-energy landscape and thus determines the folding pathway and the rate constants of folding and unfolding, as well as the protein's native structure. Theory has shown that roughness in the energy landscape will lead to slower folding, but derivation of detailed experimental descriptions of this landscape is challenging. Simple folding models show that folding is significantly influenced by chain entropy; proteins in which the contacts are local fold quickly, owing to the low entropy cost of forming stabilizing, native contacts during folding. For some protein families, stability is al

SUBMITTER: Wensley BG 

PROVIDER: S-EPMC2851140 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature