Dynamics of myoglobin: comparison of simulation results with neutron scattering spectra.
Molecular dynamics simulations are used to calculate the incoherent neutron scattering spectra of myoglobin between 80 K and 325 K and compared with experimental data. There is good agreement over the entire temperature range for the elastic, quasi-elastic, and inelastic components of the scattering. This provides support for the accuracy of the simulations of the internal motions that make the dominant contributions to the atomic displacements on a time scale of 0.3-100 ps (100-0.3 cm-1). Analysis of the simulations shows that at low temperatures a harmonic description of the molecule is appropriate and that the molecule is trapped in localized regions of conformational space. At higher temperatures the scattering arises from a combination of vibrations within wells (substates) and transitions between them; the latter contribute to the quasi-elastic scattering.
Smith
J
J
Chemistry Department, Harvard University, Cambridge, MA 01238.
Kuczera
K
K
Karplus
M
M
D003198:Computer Simulation; D009211:Myoglobin / Q000378:metabolism*; D009502:Neutrons; D011487:Protein Conformation; D012542:Scattering, Radiation; D013816:Thermodynamics
D009211:Myoglobin