title: Liquid-like side-chain dynamics in myoglobin.
abstract: At temperatures above approximately 200 K the motions of atoms in globular proteins contain a non-vibrational component that gives rise to characteristic elastic and quasi-elastic neutron scattering profiles. There is evidence that the non-vibrational dynamics is required for protein function. Here we show by analysing a molecular dynamics simulation of myoglobin that the neutron scattering results from liquid-like rigid-body motion of the protein side-chains.
authors.affiliation: IBM France, Paris.
authors.forename: G R
authors.initials: GR
authors.lastname: Kneller
authors.forename: J C
authors.initials: JC
authors.lastname: Smith
mesh_terms: D003198:Computer Simulation; D015394:Molecular Structure; D009211:Myoglobin / Q000737:chemistry*; D009502:Neutrons; D012542:Scattering, Radiation; D013816:Thermodynamics
chemical_list: D009211:Myoglobin