Probing the folding transition state structure of the villin headpiece subdomain via side chain and backbone mutagenesis.

ABSTRACT: Backbone-backbone hydrogen bonds are a common feature of native protein structures, yet their thermodynamic and kinetic influence on folding has long been debated. This is reflected by the disparity between current protein folding models, which place hydrogen bond formation at different stages along the folding trajectory. For example, previous studies have suggested that the denatured state of the villin headpiece subdomain contains a residual helical structure that may provide a bias toward the folded state by confining the conformational search associated with its folding. Although helical hydrogen bonds clearly stabilize the folded state, here we show, using an amide-to-ester mutation strategy, that the formation of backbone hydrogen bonds within helices is not rate-limiting in the fol

SUBMITTER: Bunagan MR 

PROVIDER: S-EPMC2754817 | biostudies-literature | 2009 Jun

REPOSITORIES: biostudies-literature