Low-temperature inflection observed in neutron scattering measurements of proteins is due to methyl rotation: direct evidence using isotope labeling and molecular dynamics simulations

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dc.contributor.authorWood, Ken_AU
dc.contributor.authorTobias, DJen_AU
dc.contributor.authorKessler, Ben_AU
dc.contributor.authorGabel, Fen_AU
dc.contributor.authorOesterhelt, Den_AU
dc.contributor.authorMulder, FAAen_AU
dc.contributor.authorZaccai, Gen_AU
dc.contributor.authorWeik, Men_AU
dc.date.accessioned2010-07-02T06:23:39Zen_AU
dc.date.available2010-07-02T06:23:39Zen_AU
dc.date.issued2010-04-14en_AU
dc.date.statistics2010-04-14en_AU
dc.description.abstractThere is increasing interest in the contribution of methyl groups to the overall dynamics measured by neutron scattering experiments of proteins. In particular an inflection observed in atomic mean square displacements measured as a function of temperature on high resolution spectrometers (~1 μeV) was explained by the onset of methyl group rotations. By specifically labeling a non-methyl-containing side-chain in a native protein system, the purple membrane, and performing neutron scattering measurements, we here provide direct experimental evidence that the observed inflection is indeed due to methyl group rotations. Molecular dynamics simulations reproduce the experimental data, and their analysis suggests that the apparent transition is due to methyl group rotation entering the finite instrumental resolution of the spectrometer. Methyl group correlation times measured by solid state NMR in the purple membrane, taken from previous work, support the interpretation. © 2010, American Chemical Societyen_AU
dc.identifier.citationWood, K., Tobias, D. J., Kessler, B., Gabel, F., Oesterhelt, D., Mulder, F. A. A., Zaccai, G., & Weik, M. (2010). Low-temperature inflection observed in neutron scattering measurements of proteins is due to methyl rotation: direct evidence using isotope labeling and molecular dynamics simulations. Journal of the American Chemical Society, 132(14), 4990-4991. doi:10.1021/ja910502gen_AU
dc.identifier.govdoc1824en_AU
dc.identifier.issn0002-7863en_AU
dc.identifier.issue14en_AU
dc.identifier.journaltitleJournal of the American Chemical Societyen_AU
dc.identifier.pagination4990-4991en_AU
dc.identifier.urihttp://dx.doi.org/10.1021/ja910502gen_AU
dc.identifier.urihttp://apo.ansto.gov.au/dspace/handle/10238/1726en_AU
dc.identifier.volume132en_AU
dc.language.isoenen_AU
dc.publisherAmerican Chemical Societyen_AU
dc.subjectMolecular dynamics methoden_AU
dc.subjectProteinsen_AU
dc.subjectSpectrometersen_AU
dc.subjectScatteringen_AU
dc.subjectRotationen_AU
dc.subjectTemperature rangeen_AU
dc.titleLow-temperature inflection observed in neutron scattering measurements of proteins is due to methyl rotation: direct evidence using isotope labeling and molecular dynamics simulationsen_AU
dc.typeJournal Articleen_AU
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