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@ARTICLE{Schir:188918,
      author       = {Schirò, Giorgio and Fichou, Yann and Gallat,
                      Francois-Xavier and Wood, Kathleen and Gabel, Frank and
                      Moulin, Martine and Härtlein, Michael and Heyden, Matthias
                      and Colletier, Jacques-Philippe and Orecchini, Andrea and
                      Paciaroni, Alessandro and Wuttke, Joachim and Tobias,
                      Douglas J. and Weik, Martin},
      title        = {{T}ranslational diffusion of hydration water correlates
                      with functional motions in folded and intrinsically
                      disordered proteins},
      journal      = {Nature Communications},
      volume       = {6},
      issn         = {2041-1723},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2015-02214},
      pages        = {6490},
      year         = {2015},
      abstract     = {Hydration ​water is the natural matrix of biological
                      macromolecules and is essential for their activity in cells.
                      The coupling between ​water and protein dynamics has been
                      intensively studied, yet it remains controversial. Here we
                      combine protein perdeuteration, neutron scattering and
                      molecular dynamics simulations to explore the nature of
                      hydration ​water motions at temperatures between 200 and
                      300 K, across the so-called protein dynamical transition,
                      in the intrinsically disordered human protein ​tau and the
                      globular ​maltose binding protein. Quasi-elastic
                      broadening is fitted with a model of translating, rotating
                      and immobile ​water molecules. In both experiment and
                      simulation, the translational component markedly increases
                      at the protein dynamical transition (around 240 K),
                      regardless of whether the protein is intrinsically
                      disordered or folded. Thus, we generalize the notion that
                      the translational diffusion of ​water molecules on a
                      protein surface promotes the large-amplitude motions of
                      proteins that are required for their biological activity.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1 /
                      JCNS-2},
      ddc          = {500},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)SPHERES-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000352719300003},
      pubmed       = {pmid:25774711},
      doi          = {10.1038/ncomms7490},
      url          = {https://juser.fz-juelich.de/record/188918},
}