title: Protein-water displacement distributions.
abstract: The statistical properties of fast protein-water motions are analyzed by dynamic neutron scattering experiments. Using isotopic exchange, one probes either protein or water hydrogen displacements. A moment analysis of the scattering function in the time domain yields model-independent information such as time-resolved mean square displacements and the Gauss-deviation. From the moments, one can reconstruct the displacement distribution. Hydration water displays two dynamical components, related to librational motions and anomalous diffusion along the protein surface. Rotational transitions of side chains, in particular of methyl groups, persist in the dehydrated and in the solvent-vitrified protein structure. The interaction with water induces further continuous protein motions on a small scale. Water acts as a plasticizer of displacements, which couple to functional processes such as open-closed transitions and ligand exchange.
authors.affiliation: Technische Universität München, Physik Department E 13, Garching, Germany. wdoster@ph.tum.de
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Doster
authors.forename: Marcus
authors.initials: M
authors.lastname: Settles
mesh_terms: D055592:Biophysical Phenomena; D001703:Biophysics; D008956:Models, Chemical; D033363:Neutron Diffraction; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
chemical_list: D011506:Proteins; D012997:Solvents; D014867:Water