Transition states in protein folding kinetics: modeling phi-values of small beta-sheet proteins.

ABSTRACT: Small single-domain proteins often exhibit only a single free-energy barrier, or transition state, between the denatured and the native state. The folding kinetics of these proteins is usually explored via mutational analysis. A central question is which structural information on the transition state can be derived from the mutational data. In this article, we model and structurally interpret mutational Phi-values for two small beta-sheet proteins, the PIN and the FBP WW domains. The native structure of these WW domains comprises two beta-hairpins that form a three-stranded beta-sheet. In our model, we assume that the transition state consists of two conformations in which either one of the hairpins is formed. Such a transition state has been recently observed in molecular dynamics folding

SUBMITTER: Weikl TR 

PROVIDER: S-EPMC2186242 | biostudies-literature | 2008 Feb

REPOSITORIES: biostudies-literature