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@ARTICLE{Gallat:22575,
      author       = {Gallat, F.-X. and Laganowska, A. and Wood, K. and Gabel, F.
                      and van Eijck, L. and Wuttke, J. and Moulin, M. and
                      Härtlein, M. and Eisenberg, D. and Colletier, J.-P. and
                      Zaccai, G. and Weik, M.},
      title        = {{D}ynamical {C}oupling of {I}ntrinsically {D}isordered
                      {P}roteins and {T}heir {H}ydration {W}ater: {C}omparison
                      with {F}olded {S}oluble and {M}embrane {P}roteins},
      journal      = {Biophysical journal},
      volume       = {103},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-22575},
      pages        = {129 - 136},
      year         = {2012},
      note         = {This work was supported by the Commissariat a l'Energie
                      Atomique et aux Energies Alternatives, Centre National de la
                      Recherche Scientifique, Universite Joseph Fourier, and
                      Agence Nationale de la Recherche (project number
                      ANR-11-BSV5-027 to M. W.). This work benefited from the
                      activities of the DLAB consortium funded by the European
                      Union under contracts HPRI-2001-50065 and
                      RII3-CT-2003-505925, and from UK Engineering and Physical
                      Sciences Research Council-funded activity within the
                      ILL-EMBL Deuteration Laboratory under grants GR/R99393/01
                      and EP/C015452/1. The study was also supported by the
                      European Commission under the 7th Framework Programme
                      through the Research Infrastructures action of the
                      Capacities Programme, contract $CP-CSA_INFRA-2008-1.1.1$
                      number 226507-NMI3. K. W. acknowledges funding from the
                      Access to Major Research Facilities Program, supported by
                      the Commonwealth of Australia under the International
                      Science Linkages Program.},
      abstract     = {Hydration water is vital for various macromolecular
                      biological activities, such as specific ligand recognition,
                      enzyme activity, response to receptor binding, and energy
                      transduction. Without hydration water, proteins would not
                      fold correctly and would lack the conformational flexibility
                      that animates their three-dimensional structures. Motions in
                      globular, soluble proteins are thought to be governed to a
                      certain extent by hydration-water dynamics, yet it is not
                      known whether this relationship holds true for other protein
                      classes in general and whether, in turn, the structural
                      nature of a protein also influences water motions. Here, we
                      provide insight into the coupling between hydration-water
                      dynamics and atomic motions in intrinsically disordered
                      proteins (IDP), a largely unexplored class of proteins that,
                      in contrast to folded proteins, lack a well-defined
                      three-dimensional structure. We investigated the human IDP
                      tau, which is involved in the pathogenic processes
                      accompanying Alzheimer disease. Combining neutron scattering
                      and protein perdeuteration, we found similar atomic
                      mean-square displacements over a large temperature range for
                      the tau protein and its hydration water, indicating intimate
                      coupling between them. This is in contrast to the behavior
                      of folded proteins of similar molecular weight, such as the
                      globular, soluble maltose-binding protein and the membrane
                      protein bacteriorhodopsin, which display moderate to weak
                      coupling, respectively. The extracted mean square
                      displacements also reveal a greater motional flexibility of
                      IDP compared with globular, folded proteins and more
                      restricted water motions on the IDP surface. The results
                      provide evidence that protein and hydration-water motions
                      mutually affect and shape each other, and that there is a
                      gradient of coupling across different protein classes that
                      may play a functional role in macromolecular activity in a
                      cellular context.},
      keywords     = {J (WoSType)},
      cin          = {ICS-1 / JCNS (München) ; Jülich Centre for Neutron
                      Science JCNS (München) ; JCNS-FRM-II / JCNS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung (FUEK505) / 544 - In-house Research
                      with PNI (POF2-544) / NMI3 - Integrated Infrastructure
                      Initiative for Neutron Scattering and Muon Spectroscopy
                      (226507)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-HGF)POF2-544 /
                      G:(EU-Grant)226507},
      experiment   = {EXP:(DE-MLZ)SPHERES-20140101},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22828339},
      pmc          = {pmc:PMC3388209},
      UT           = {WOS:000306088800020},
      doi          = {10.1016/j.bpj.2012.05.027},
      url          = {https://juser.fz-juelich.de/record/22575},
}