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dc.contributor.authorBecker, Torsten
dc.contributor.authorHayward, Jennifer A.
dc.contributor.authorFinney, John L.
dc.contributor.authorDaniel, Roy M.
dc.contributor.authorSmith, Jeremy C.
dc.date.accessioned2008-11-07T01:15:18Z
dc.date.available2008-11-07T01:15:18Z
dc.date.issued2004-09
dc.identifier.citationBecker, T., Hayward, J. A., Finney, J. L., Daniel, R. M. & Smith, J. (2004). Neutron frequency windows and the protein dynamical transition. Biophysical Journal, 87, 1436-1444.en_US
dc.identifier.issn1542-0086
dc.identifier.urihttps://hdl.handle.net/10289/1291
dc.description.abstractProteins undergo an apparent dynamical transition on temperature variation that has been correlated with the onset of function. The transition in the mean-square displacement, ∆r2 , that is observed using a spectrometer or computer simulation, depends on the relationship between the timescales of the relaxation processes activated and the timescale accessible to the instrument or simulation. Models are described of two extreme situations—an "equilibrium" model, in which the long-time dynamics changes with temperature and all motions are resolved by the instrument used; and a "frequency window" model, in which there is no change in the long-time dynamics but as the temperature increases, the relaxation frequencies move into the instrumental range. Here we demonstrate that the latter, frequency-window model can describe the temperature and timescale dependences of both the intermediate neutron scattering function and ∆r2 derived from molecular dynamics simulations of a small protein in a cryosolution. The frequency-window model also describes the energy-resolution and temperature-dependences of ∆r2 obtained from experimental neutron scattering on glutamate dehydrogenase in the same solvent. Although equilibrium effects should also contribute to dynamical transitions in proteins, the present results suggests that frequency-window effects can play a role in the simulations and experiments examined. Finally, misquotations of previous findings are discussed in the context of solvent activation of protein dynamics and the possible relationship of this to activity.en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen
dc.publisherBiophysical Societyen_NZ
dc.relation.urihttp://www.biophysj.org/cgi/content/abstract/87/3/1436en_US
dc.rightsThis article has been published in the journal: Biophysical Journal. Copyright © 2004 by the Biophysical Society.en_US
dc.titleNeutron frequency windows and the protein dynamical transitionen_US
dc.typeJournal Articleen_US
dc.relation.isPartOfBiophysical Journalen_NZ
pubs.begin-page1en_NZ
pubs.editionSeptemberen_NZ
pubs.elements-id30625
pubs.end-page9en_NZ
pubs.issue3en_NZ
pubs.volume87en_NZ


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