title: Unifying microscopic mechanism for pressure and cold denaturations of proteins.
abstract: We study the stability of globular proteins as a function of temperature and pressure through NPT simulations of a coarse-grained model. We reproduce the elliptical stability of proteins and highlight a unifying microscopic mechanism for pressure and cold denaturations. The mechanism involves the solvation of nonpolar residues with a thin layer of water. These solvated states have lower volume and lower hydrogen-bond energy compared to other conformations of nonpolar solutes. Hence, these solvated states are favorable at high pressure and low temperature, and they facilitate protein unfolding under these thermodynamical conditions.
authors.affiliation: Fachbereich Physik, Freie Universität Berlin, Arnimalle 14, 14195 Berlin, Germany.
authors.forename: Cristiano L
authors.initials: CL
authors.lastname: Dias
mesh_terms: D003080:Cold Temperature; D057927:Hydrophobic and Hydrophilic Interactions; D008853:Microscopy / Q000379:methods; D008956:Models, Chemical; D011312:Pressure; D011487:Protein Conformation; D011489:Protein Denaturation; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D011506:Proteins; D014867:Water