title: Possible mechanism underlying high-pressure unfolding of proteins: formation of a short-period high-density hydration shell.
abstract: Hydration effects on high-pressure unfolding of a hydrophobic polymer chain are investigated through a multiscale simulation based on density-functional theory. The results strongly suggest the following: a thermodynamic origin for high-pressure denaturation, i.e., the decrease in volume due to the unfolding can be explained by the formation of a short-period high-density hydration shell.
authors.affiliation: Department of Computer Science and Engineering, Toyohashi University of Technology, Tempaku-cho, Toyohashi 441-8580, Japan. sumi@tut.jp
authors.forename: Tomonari
authors.initials: T
authors.lastname: Sumi
authors.forename: Hideo
authors.initials: H
authors.lastname: Sekino
mesh_terms: D057927:Hydrophobic and Hydrophilic Interactions; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D011506:Proteins; D014867:Water