Making connections between ultrafast protein folding kinetics and molecular dynamics simulations.

ABSTRACT: Determining the rate of forming the truly folded conformation of ultrafast folding proteins is an important issue for both experiments and simulations. The double-norleucine mutant of the 35-residue villin subdomain is the focus of recent computer simulations with atomistic molecular dynamics because it is currently the fastest folding protein. The folding kinetics of this protein have been measured in laser temperature-jump experiments using tryptophan fluorescence as a probe of overall folding. The conclusion from the simulations, however, is that the rate determined by fluorescence is significantly larger than the rate of overall folding. We have therefore employed an independent experimental method to determine the folding rate. The decay of the tryptophan triplet-state in photoselecti

SUBMITTER: Cellmer T 

PROVIDER: S-EPMC3076883 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature