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The Glass Transition in Proteins

In: High Performance Computing in Science and Engineering ’02

Author

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  • Jennifer A. Hayward

    (Universität Heidelberg, IWR)

  • Torsten Becker

    (Universität Heidelberg, IWR)

  • Jeremy C. Smith

    (Universität Heidelberg, IWR)

Abstract

The temperature dependence of the internal dynamics of an isolated protein, bovine pancreatic trypsin inhibitor, is examined using normal mode analysis (NMA) and molecular dynamics (MD) simulation. It is found that this model exhibits marked anharmonic dynamics, at temperatures much lower than previously detected in proteins, as evidenced by departure from the harmonic model mean- square displacement. A new method for determining mean-square displacements from elastic incoherent neutron scattering experiments is demonstrated and it is found to be more accurate than the method currently used by experimentalists.

Suggested Citation

  • Jennifer A. Hayward & Torsten Becker & Jeremy C. Smith, 2003. "The Glass Transition in Proteins," Springer Books, in: Egon Krause & Willi Jäger (ed.), High Performance Computing in Science and Engineering ’02, pages 503-511, Springer.
    • Handle: RePEc:spr:sprchp:978-3-642-59354-3_40
    DOI: 10.1007/978-3-642-59354-3_40
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