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@ARTICLE{Doster:201056,
      author       = {Doster, Wolfgang and Gutberlet, Thomas},
      title        = {{T}he {P}rotein-{W}ater {E}nergy {S}eascape},
      journal      = {Biochimica et biophysica acta / Proteins and proteomics},
      volume       = {1804},
      number       = {1},
      issn         = {1570-9639},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2015-03366},
      pages        = {1 - 2},
      year         = {2010},
      abstract     = {Protein molecules and liquid water are very different
                      systems both from a structural and a dynamic point of view.
                      Proteins are long range ordered, but its local molecular
                      motions are restricted by covalent bonds, which makes it
                      solid-like. The dynamics of such a system is properly
                      represented by barrier crossing within a well defined energy
                      landscape. Water in contrast is short-range ordered, but
                      long range diffusion allows it to flow, the essence of the
                      liquid state. The energy landscape is thus fluctuating and
                      motion is determined by collective reorganization of
                      molecules forming transient holes, the landscape turns into
                      a seascape. At the protein-water interface mutual
                      interactions modify the properties of both systems. The
                      protein landscape is modulated in time by density
                      fluctuations in the liquid phase and interfacial water is
                      transiently immobilized by rigid protein structure.The
                      physical phenomenon of protein hydration is to some extent
                      elusive, since there is no rigid shell of water around a
                      protein molecule. Instead there is a fluctuating cloud which
                      is thermodynamically and dynamically different from bulk
                      water. A “hydrodynamic” definition of hydration water is
                      to evaluate, how many water molecules near the protein
                      surface have their displacement vector along the trajectory
                      of the protein at any instant of time. This is determined by
                      the strength of interaction with the protein and, hence, by
                      the ratio of the time that is spent “attached” to the
                      protein to the time spent in the bulk phase. The sum of the
                      fractional contributions of all water molecules is the
                      measured hydration. It is the mass of water, which migrates
                      with the protein at any instant of time. When divided by the
                      molecular weight of water, this yields the average number of
                      molecules, which interact with the protein [1].An
                      operational definition is to determine the amount of
                      non-freezable water at low temperatures, which depends
                      however on the cooling-rate if crystallization occurs. Below
                      about 0.4 g water per g protein, crystallization is
                      hindered. The hydration shell can be super-cooled until a
                      glass transition interferes at 170 K. In such hydrated
                      protein powders, the water molecules are permanently in
                      contact with the protein surface, while protein translation
                      and rotation is suppressed. Such surface-attached water
                      molecules are still highly mobile, performing long-range
                      diffusion, which is a property of the liquid state. The
                      translational diffusion is arrested at the glass transition
                      [2]. This dramatic slowing down of molecular motions of
                      water is a useful approach to the coupling between water and
                      protein dynamics},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1 /
                      JCNS-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106},
      pnm          = {54G - JCNS (POF2-54G24)},
      pid          = {G:(DE-HGF)POF2-54G24},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000272765200001},
      doi          = {10.1016/j.bbapap.2009.11.003},
      url          = {https://juser.fz-juelich.de/record/201056},
}