A Tale of Two Desolvation Potentials: An Investigation of Protein Behavior under High Hydrostatic Pressure.

ABSTRACT: Hydrostatic pressure is a common perturbation to probe the conformations of proteins. There are two common forms of pressure-dependent potentials of mean force (PMFs) derived from hydrophobic molecules available for coarse-grained molecular simulations of protein folding and unfolding under hydrostatic pressure. Although both PMFs include a desolvation barrier separating the direct contact well and the solvent-mediated contact well, how these features vary with hydrostatic pressure is still debated. There is a need for a systematic comparison of these two PMFs on a protein. We investigated the two different pressure-dependencies on the desolvation potential in a structure-based protein model using coarse-grained molecular simulations. We compared the simulation results to the known behavio

SUBMITTER: Gasic AG 

PROVIDER: S-EPMC8691387 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature