Side chain burial and hydrophobic core packing in protein folding transition states.

ABSTRACT: A critical step in the folding pathway of globular proteins is the formation of a tightly packed hydrophobic core. Several mutational studies have addressed the question of whether tight packing interactions are present during the rate-limiting step of folding. In some of these investigations, substituted side chains have been assumed to form native-like interactions in the transition state when the folding rates of mutant proteins correlate with their native-state stabilities. Alternatively, it has been argued that side chains participate in nonspecific hydrophobic collapse when the folding rates of mutant proteins correlate with side-chain hydrophobicity. In a reanalysis of published data, we have found that folding rates often correlate similarly well, or poorly, with both native-state

SUBMITTER: Farber PJ 

PROVIDER: S-EPMC2271162 | biostudies-literature | 2008 Apr

REPOSITORIES: biostudies-literature