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. 1990 Feb;87(4):1601–1605. doi: 10.1073/pnas.87.4.1601

Dynamics of myoglobin: comparison of simulation results with neutron scattering spectra.

J Smith 1, K Kuczera 1, M Karplus 1
PMCID: PMC53523  PMID: 2304919

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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