Empirical Optimization of Interactions between Proteins and Chemical Denaturants in Molecular Simulations.

ABSTRACT: Chemical denaturants are the most commonly used perturbation applied to study protein stability and folding kinetics as well as the properties of unfolded polypeptides. We build on recent work balancing the interactions of proteins and water, and accurate models for the solution properties of urea and guanidinium chloride, to develop a combined force field that is able to capture the strength of interactions between proteins and denaturants. We use solubility data for a model tetraglycine peptide in each denaturant to tune the protein-denaturant interaction by a novel simulation methodology. We validate the results against data for more complex sequences: single-molecule Förster resonance energy transfer data for a 34-residue fragment of the globular protein CspTm and photoinduced electron

SUBMITTER: Zheng W 

PROVIDER: S-EPMC6139257 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature