Correlation analysis for heat denaturation of Trp-cage miniprotein with explicit solvent.

ABSTRACT: Energetics was analyzed for Trp-cage miniprotein in water to elucidate the solvation effect in heat denaturation. The solvation free energy was computed for a set of protein structures at room and high temperatures with all-atom molecular dynamics simulation combined with the solution theory in the energy representation, and its correlations were investigated against the intramolecular (structural) energy of the protein and the average interaction energy of the protein with the solvent water. It was observed both at room and high temperatures that the solvation free energy is anticorrelated to the structural energy and varies in parallel to the electrostatic component of the protein-water interaction energy without correlations to the van der Waals and excluded-volume components. When the

SUBMITTER: Kamo F 

PROVIDER: S-EPMC4815324 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature