title: High-resolution free energy landscape analysis of protein folding.
abstract: The free energy landscape can provide a quantitative description of folding dynamics, if determined as a function of an optimally chosen reaction coordinate. The profile together with the optimal coordinate allows one to directly determine such basic properties of folding dynamics as the configurations of the minima and transition states, the heights of the barriers, the value of the pre-exponential factor and its relation to the transition path times. In the present study, we review the framework, in particular, the approach to determine such an optimal coordinate, and its application to the analysis of simulated protein folding dynamics.
authors: *Astbury Center for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, U.K.
authors: Polina V
authors: PV
authors: Banushkina
authors: *Astbury Center for Structural Molecular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, U.K.
authors: Sergei V
authors: SV
authors: Krivov
mesh_terms: D003198:Computer Simulation; D007700:Kinetics; D008958:Models, Molecular; D017510:Protein Folding; D013816:Thermodynamics