Comparing Fast Pressure Jump and Temperature Jump Protein Folding Experiments and Simulations.

ABSTRACT: The unimolecular folding reaction of small proteins is now amenable to a very direct mechanistic comparison between experiment and simulation. We present such a comparison of microsecond pressure and temperature jump refolding kinetics of the engineered WW domain FiP35, a model system for β-sheet folding. Both perturbations produce experimentally a faster and a slower kinetic phase, and the "slow" microsecond phase is activated. The fast phase shows differences between perturbation methods and is closer to the downhill limit by temperature jump, but closer to the transiently populated intermediate limit by pressure jump. These observations make more demands on simulations of the folding process than just a rough comparison of time scales. To complement experiments, we carried out several p

SUBMITTER: Wirth AJ 

PROVIDER: S-EPMC4794261 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature