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Protein Surface and Core Dynamics Show Concerted Hydration-Dependent Activation

Authors

  • Dr. Kathleen Wood,

    1. Australian Nuclear Science and Technology Organisation Bragg Institute, Menai NSW (Australia)
    2. Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, (The Netherlands)
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    • These authors contributed equally to this work.

  • Dr. François-Xavier Gallat,

    1. Institut Laue Langevin, Grenoble (France)
    2. Comissariat à l'Energie Atomique, 38054 Grenoble (France) and CNRS, UMR5075, 38027 Grenoble (France) and Université Joseph Fourier, 38000 Grenoble (France)
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    • These authors contributed equally to this work.

  • Dr. Renee Otten,

    1. Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, (The Netherlands)
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    • These authors contributed equally to this work.

  • Auke J. van Heel,

    1. Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, (The Netherlands)
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  • Mathilde Lethier,

    1. Institut Laue Langevin, Grenoble (France)
    2. Comissariat à l'Energie Atomique, 38054 Grenoble (France) and CNRS, UMR5075, 38027 Grenoble (France) and Université Joseph Fourier, 38000 Grenoble (France)
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  • Dr. Lambert van Eijck,

    1. Institut Laue Langevin, Grenoble (France)
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  • Martine Moulin,

    1. Institut Laue Langevin, Grenoble (France)
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  • Dr. Michael Haertlein,

    1. Institut Laue Langevin, Grenoble (France)
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  • Dr. Martin Weik,

    1. Comissariat à l'Energie Atomique, 38054 Grenoble (France) and CNRS, UMR5075, 38027 Grenoble (France) and Université Joseph Fourier, 38000 Grenoble (France)
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  • Prof. Dr. Frans A. A. Mulder

    Corresponding author
    1. Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, University of Aarhus, Langelandsgade 140, 8000 Aarhus C (Denmark) http://bionmr.chem.au.dk
    2. Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, (The Netherlands)
    • Interdisciplinary Nanoscience Center (iNANO) and Department of Chemistry, University of Aarhus, Langelandsgade 140, 8000 Aarhus C (Denmark) http://bionmr.chem.au.dk
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  • This work has benefitted from the activities of the DLAB consortium funded by the EU under contracts HPRI-2001-50065 and RII3-CT-2003-505925, and from UK EPSRC-funded activity under grants GR/R99393/01 and EP/C015452/1. The authors thank the ILL for beamtime, Bernhard Frick for his continuous support, and Giuseppe Zaccai for fruitful discussions. M.W. and F.A.A.M. thank EGIDE and NWO for funding. K.W. acknowledges funding from the access to major research facilities program, supported by the Commonwealth of Australia under the International Science Linkages program. Financial support by the CEA, the CNRS, and the UJF is acknowledged, as well as a grant from the Agence Nationale de la Recherche (grant number ANR-11-BSV5-027) to M.W. and an ILL PhD fellowship to F.X.G.

Abstract

original image

By specifically labeling leucine/valine methyl groups and lysine side chains “inside” and “outside” dynamics of proteins on the nanosecond timescale are compared using neutron scattering (see picture). Surprisingly, both groups display similar dynamics as a function of temperature, and the buried hydrophobic core is sensitive to hydration and undergoes a dynamical transition.

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