Research Commons
      • Browse 
        • Communities & Collections
        • Titles
        • Authors
        • By Issue Date
        • Subjects
        • Types
        • Series
      • Help 
        • About
        • Collection Policy
        • OA Mandate Guidelines
        • Guidelines FAQ
        • Contact Us
      • My Account 
        • Sign In
        • Register
      View Item 
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      •   Research Commons
      • University of Waikato Research
      • Science and Engineering
      • Science and Engineering Papers
      • View Item
      JavaScript is disabled for your browser. Some features of this site may not work without it.

      Neutron frequency windows and the protein dynamical transition

      Becker, Torsten; Hayward, Jennifer A.; Finney, John L.; Daniel, Roy M.; Smith, Jeremy C.
      Thumbnail
      Files
      Biophy Neutron.pdf
      150.4Kb
      Link
       www.biophysj.org
      Find in your library  
      Citation
      Export citation
      Becker, 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.
      Permanent Research Commons link: https://hdl.handle.net/10289/1291
      Abstract
      Proteins 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.
      Date
      2004-09
      Type
      Journal Article
      Publisher
      Biophysical Society
      Rights
      This article has been published in the journal: Biophysical Journal. Copyright © 2004 by the Biophysical Society.
      Collections
      • Science and Engineering Papers [3124]
      Show full item record  

      Usage

      Downloads, last 12 months
      63
       
       

      Usage Statistics

      For this itemFor all of Research Commons

      The University of Waikato - Te Whare Wānanga o WaikatoFeedback and RequestsCopyright and Legal Statement