title: Three classes of motion in the dynamic neutron-scattering susceptibility of a globular protein.
abstract: A simplified description of the 295 K dynamics of a globular protein over a wide frequency range (1-1000 GHz) is obtained by combining neutron scattering of lysozyme with molecular dynamics simulation. The molecular dynamics simulation agrees quantitatively with experiment for both the protein and the hydration water and shows that, whereas the hydration water molecules subdiffuse, the protein atoms undergo confined motion decomposable into three distinct classes: localized diffusion, methyl group rotations, and jumps. Each of the three classes gives rise to a characteristic neutron susceptibility signal.
authors: University of Tennessee/Oak Ridge National Laboratory Center for Molecular Biophysics, P.O.Box 2008, Oak Ridge Tennessee 37831-6164, USA.
authors: Liang
authors: L
authors: Hong
authors: Nikolai
authors: N
authors: Smolin
authors: Benjamin
authors: B
authors: Lindner
authors: Alexei P
authors: AP
authors: Sokolov
authors: Jeremy C
authors: JC
authors: Smith
mesh_terms: D056004:Molecular Dynamics Simulation; D009068:Movement; D009113:Muramidase / Q000737:chemistry* / Q000378:metabolism*; D033363:Neutron Diffraction; D014867:Water / Q000737:chemistry
chemical_list: D014867:Water; D009113:Muramidase