Abstract
The derivation of mean-square displacements from elastic incoherent neutron scattering (EINS) of proteins is examined, with the aid of experiments on camphor-bound cytochrome P450cam and complementary molecular dynamics simulations. It is shown that a q4 correction to the elastic incoherent structure factor (where q is the scattering vector) can be simply used to reliably estimate from the experiment both the average mean-square atomic displacement (MSD) of the non-exchanged hydrogen atoms in the protein and its variance. The molecular dynamics simulation results are in broad agreement with the experimentally-derived MSD and its variance derived from EINS on instruments at two different energy resolutions, corresponding to dynamics on the ∼100 ps and ∼1 ns timescales. Significant dynamical heterogeneity is found to arise from methyl-group rotations. The easy-to-apply q4 correction extends the information extracted from elastic incoherent neutron scattering experiments and should be of wide applicability.
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