Probing the Action of Chemical Denaturant on an Intrinsically Disordered Protein by Simulation and Experiment.

ABSTRACT: Chemical denaturants are the most commonly used agents for unfolding proteins and are thought to act by better solvating the unfolded state. Improved solvation is expected to lead to an expansion of unfolded chains with increasing denaturant concentration, providing a sensitive probe of the denaturant action. However, experiments have so far yielded qualitatively different results concerning the effects of chemical denaturation. Studies using Förster resonance energy transfer (FRET) and other methods found an increase in radius of gyration with denaturant concentration, but most small-angle X-ray scattering (SAXS) studies found no change. This discrepancy therefore challenges our understanding of denaturation mechanism and more generally the accuracy of these experiments as applied to unfo

SUBMITTER: Zheng W 

PROVIDER: S-EPMC5597963 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature