title: Role of protein-water hydrogen bond dynamics in the protein dynamical transition.
abstract: The role of water in protein dynamics has been investigated using molecular dynamics simulations of crystals and a dehydrated powder. On the 100 ps time scale, the anharmonic and diffusive motions involved in the protein structural relaxation are correlated with the protein-water hydrogen bond dynamics. The complete structural relaxation of the protein requires relaxation of the hydrogen bond network via solvent translational displacement. Inhibiting the solvent translational mobility, and therefore the protein-water hydrogen bond dynamics, has an effect on the protein relaxation similar to dehydration.
authors.affiliation: NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899-8562, USA.
authors.forename: M
authors.initials: M
authors.lastname: Tarek
authors.forename: D J
authors.initials: DJ
authors.lastname: Tobias
mesh_terms: D003080:Cold Temperature; D003198:Computer Simulation; D003890:Desiccation; D006860:Hydrogen Bonding; D011312:Pressure; D012259:Ribonuclease, Pancreatic / Q000737:chemistry*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry*
chemical_list: D014867:Water; D012259:Ribonuclease, Pancreatic