Coincidence of dynamical transitions in a soluble protein and its hydration water: direct measurements by neutron scattering and MD simulations.
The coupling between protein dynamics and hydration-water dynamics was assessed by perdeuteration, temperature-dependent neutron scattering, and molecular dynamics simulations. Mean square displacements of water and protein motions both show a broad transition at 220 K and are thus coupled. In particular, the protein dynamical transition appears to be driven by the onset of hydration-water translational motion.
Wood
Kathleen
K
Laboratoire de Biophysique Moléculaire, Institut de Biologie Structurale, Jean Pierre EBEL, 41 rue Jules Horowitz, F-38027 Grenoble, France.
Frölich
Andreas
A
Paciaroni
Alessandro
A
Moulin
Martine
M
Härtlein
Michael
M
Zaccai
Giuseppe
G
Tobias
Douglas J
DJ
Weik
Martin
M
D002352:Carrier Proteins / Q000737:chemistry*; D003198:Computer Simulation; D003903:Deuterium / Q000737:chemistry; D058619:Maltose-Binding Proteins; D033363:Neutron Diffraction / Q000379:methods; D013696:Temperature; D014867:Water / Q000737:chemistry*
D002352:Carrier Proteins; D058619:Maltose-Binding Proteins; D014867:Water; D003903:Deuterium