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Molecular Dynamics Simulations of Protein G Challenge NMR-Derived Correlated Backbone Motions

Authors

  • Oliver F. Lange,

    1. Theoretical and Computational Biophysics Department, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany, Fax: (+49) 551-2012302
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  • Helmut Grubmüller Priv.-Doz. Dr.,

    1. Theoretical and Computational Biophysics Department, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany, Fax: (+49) 551-2012302
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  • Bert L. de Groot Dr.

    1. Theoretical and Computational Biophysics Department, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany, Fax: (+49) 551-2012302
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  • We thank Christian Griesinger, Sander Nabuurs, and Martin Stone for carefully reading the manuscript.

Abstract

original image

Correlated motions probed? A recently reported NMR relaxation experiment promised to probe correlated motions in proteins. However, molecular dynamics simulations imply that this is not the case. The simulations agree well with data obtained through two independent and established NMR spectroscopic methods and thus provide an alternative and consistent access to correlated protein motions (see picture) from NMR techniques.

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