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Solvent effects in the slow dynamics of proteins

Authors

  • Konrad Hinsen,

    Corresponding author
    1. Centre de Biophysique Moléculaire, CNRS UPR 4301, Rue Charles Sadron, 45071 Orléans Cedex 2, France
    2. Synchrotron Soleil, Saint Aubin, B.P. 48, 91192 Gif sur Yvette Cedex, France
    • Centre de Biophysique Moléculaire, CNRS UPR 4301, Rue Charles Sadron, 45071 Orléans Cedex 2, France
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  • Gerald R. Kneller

    1. Centre de Biophysique Moléculaire, CNRS UPR 4301, Rue Charles Sadron, 45071 Orléans Cedex 2, France
    2. Synchrotron Soleil, Saint Aubin, B.P. 48, 91192 Gif sur Yvette Cedex, France
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Abstract

The influence of solvent on the slow internal dynamics of proteins is studied by comparing molecular dynamics simulations of solvated and unsolvated lysozyme. The dynamical trajectories are projected onto the protein's normal modes in order to obtain a separate analysis for each of the associated time scales. The results show that solvent effects are important for the slowest motions (below ≈ 1 ps−1) but negligible for faster motions. The damping effects seen in the latter show that the principal source of friction in protein dynamics is not the solvent, but the protein itself. Proteins 2008. © 2007 Wiley-Liss, Inc.

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