Unknown

Dataset Information

0

High-Resolution Free-Energy Landscape Analysis of α-Helical Protein Folding: HP35 and Its Double Mutant.


ABSTRACT: The free-energy landscape can provide a quantitative description of folding dynamics, if determined as a function of an optimally chosen reaction coordinate. Here, we construct the optimal coordinate and the associated free-energy profile for all-helical proteins HP35 and its norleucine (Nle/Nle) double mutant, based on realistic equilibrium folding simulations [Piana et al. Proc. Natl. Acad. Sci. U.S.A.2012, 109, 17845]. From the obtained profiles, we directly determine such basic properties of folding dynamics as the configurations of the minima and transition states (TS), the formation of secondary structure and hydrophobic core during the folding process, the value of the pre-exponential factor and its relation to the transition path times, the relation between the autocorrelation times in TS and minima. We also present an investigation of the accuracy of the pre-exponential factor estimation based on the transition-path times. Four different estimations of the pre-exponential factor for both proteins give k0(-1) values of approximately a few tens of nanoseconds. Our analysis gives detailed information about folding of the proteins and can serve as a rigorous common language for extensive comparison between experiment and simulation.

SUBMITTER: Banushkina PV 

PROVIDER: S-EPMC3860327 | biostudies-other | 2013 Dec

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC5153537 | biostudies-literature
| S-EPMC9202546 | biostudies-literature
| S-EPMC2671186 | biostudies-literature
| S-EPMC6251876 | biostudies-literature
| S-EPMC4121805 | biostudies-literature
| S-EPMC2952400 | biostudies-literature
| S-EPMC263783 | biostudies-literature
| S-EPMC6797787 | biostudies-literature
| S-EPMC4968343 | biostudies-literature
| S-EPMC64961 | biostudies-literature