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Mapping the Population of Protein Conformational Energy Sub-States from NMR Dipolar Couplings

Authors

  • Dr. Paul Guerry,

    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
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    • These authors contributed equally to this work.

  • Dr. Loïc Salmon,

    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
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    • These authors contributed equally to this work.

  • Dr. Luca Mollica,

    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
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  • Dr. Jose-Luis Ortega Roldan,

    1. Department of Biochemistry, University of Oxford, South Parks Road, Oxford (UK)
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  • Dr. Phineus Markwick,

    1. Department of Chemistry and Biochemistry UCSD San Diego CA, Howard Hughes Medical Institute, San Diego Supercomputer Center, La Jolla CA (USA)
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  • Prof. Nico A. J. van Nuland,

    1. Structural Biology Brussels, Vrije Universiteit Brussel, Pleinlaan (Belgium)
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  • Prof. J. Andrew McCammon,

    1. Department of Chemistry and Biochemistry UCSD San Diego CA, Howard Hughes Medical Institute, San Diego Supercomputer Center, La Jolla CA (USA)
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  • Dr. Martin Blackledge

    Corresponding author
    1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)
    • Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CNRS-CEA-UJF UMR 5075, 41 rue Jules Horowitz, 38027 Grenoble Cedex (France)

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  • Financial support from the CEA, CNRS, UJF, ANR-12-BS07-0023-01 ComplexDynamics (M.B.), and the CCRT is acknowledged. The work at UCSD was supported by the NSF, NIH, CTBP, NBCR, and NSF Supercomputers.

Abstract

original image

Molekulare Dynamik: Eine allgemeine Methode zur Beschreibung der konformativen Energielandschaften von Proteinen in Lösung auf der Grundlage statistischer Mechanik wird vorgestellt. Die Methode beruht auf der Kombination von dipolaren NMR-Restkopplungen (RDCs), dem Abtasten des Konformationsraums durch beschleunigte Simulation der molekularen Dynamik und der Auswahl eines Ensembles unter Verwendung einer modellfreien Ensemble-Interpretation der RDCs (siehe Bild).

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