Publication Type
Journal
Journal Name
Physical Review Letters
Publication Date
Page Number
148102
Volume
107
Issue
14
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.
