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      Protein dynamics and stability: The distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering

      Meinhold, Lars; Clement, David; Tehei, Moeava; Daniel, Roy M.; Finney, John L.; Smith, Jeremy C.
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      Biophy protein.pdf
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      DOI
       10.1529/biophysj.107.121418
      Link
       www.biophysj.org
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      Meinhold, L., Clement, D., Tehei, M., Daniel, R., Finney, J. L. & Smith, J.C. (2008). Protein dynamics and stability: The distribution of atomic fluctuations in thermophilic and mesophilic dihydrofolate reductase derived using elastic incoherent neutron scattering. Biophysical Journal, 94, 4812- 4818.
      Permanent Research Commons link: https://hdl.handle.net/10289/1289
      Abstract
      The temperature dependence of the dynamics of mesophilic and thermophilic dihydrofolate reductase is examined using elastic incoherent neutron scattering. It is demonstrated that the distribution of atomic displacement amplitudes can be derived from the elastic scattering data by assuming a (Weibull) functional form that resembles distributions seen in molecular dynamics simulations. The thermophilic enzyme has a significantly broader distribution than its mesophilic counterpart. Furthermore, although the rate of increase with temperature of the atomic mean-square displacements extracted from the dynamic structure factor is found to be comparable for both enzymes, the amplitudes are found to be slightly larger for the thermophilic enzyme. Therefore, these results imply that the thermophilic enzyme is the more flexible of the two.
      Date
      2008-02
      Type
      Journal Article
      Publisher
      Biophysical Society
      Rights
      This article has been published in the journal: Biophysical Journal. Copyright © 2008 by the Biophysical Society.
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      • Science and Engineering Papers [3124]
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