Folding, misfolding, and amyloid protofibril formation of WW domain FBP28.

ABSTRACT: We study the folding mechanism of a triple beta-strand WW domain from the Formin binding protein 28 (FBP28) at atomic resolution with explicit water model using replica exchange molecular dynamics computer simulations. Extended sampling over a wide range of temperatures to obtain the free energy, enthalpy, and entropy surfaces as a function of structural coordinates has been performed. Simulations were started from different configurations covering the folded and unfolded states. In the free energy landscape a transition state is identified and its structures and -values are compared with experimental data from a homologous protein, the prolyl-isomerase Pin1 WW domain. A stable intermediate state is found to accumulate during the simulation characterized by the carboxyl-terminal beta-stran

SUBMITTER: Mu Y 

PROVIDER: S-EPMC1459504 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature