Uncovering specific electrostatic interactions in the denatured states of proteins.

ABSTRACT: The stability and folding of proteins are modulated by energetically significant interactions in the denatured state that is in equilibrium with the native state. These interactions remain largely invisible to current experimental techniques, however, due to the sparse population and conformational heterogeneity of the denatured-state ensemble under folding conditions. Molecular dynamics simulations using physics-based force fields can in principle offer atomistic details of the denatured state. However, practical applications are plagued with the lack of rigorous means to validate microscopic information and deficiencies in force fields and solvent models. This study presents a method based on coupled titration and molecular dynamics sampling of the denatured state starting from the exten

SUBMITTER: Shen JK 

PROVIDER: S-EPMC2913194 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature