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@ARTICLE{Kmpf:877757,
      author       = {Kämpf, Kerstin and Demuth, Dominik and Zamponi, Michaela
                      and Wuttke, Joachim and Vogel, Michael},
      title        = {{Q}uasielastic neutron scattering studies on couplings of
                      protein and water dynamics in hydrated elastin},
      journal      = {The journal of chemical physics},
      volume       = {152},
      number       = {24},
      issn         = {1089-7690},
      address      = {Melville, NY},
      publisher    = {American Institute of Physics},
      reportid     = {FZJ-2020-02445},
      pages        = {245101 -},
      year         = {2020},
      abstract     = {erforming quasielastic neutron scattering measurements and
                      analyzing both elastic and quasielasic contributions, we
                      study protein and water dynamics of hydrated elastin. At low
                      temperatures, hydration-independent methyl group rotation
                      dominates the findings. It is characterized by a Gaussian
                      distribution of activation energies centered at about Em =
                      0.17 eV. At ∼195 K, coupled protein–water motion sets
                      in. The hydration water shows diffusive motion, which is
                      described by a Gaussian distribution of activation energies
                      with Em = 0.57 eV. This Arrhenius behavior of water
                      diffusion is consistent with previous results for water
                      reorientation, but at variance with a fragile-to-strong
                      crossover at ∼225 K. The hydration-related elastin
                      backbone motion is localized and can be attributed to the
                      cage rattling motion. We speculate that its onset at ∼195
                      K is related to a secondary glass transition, which occurs
                      when a β relaxation of the protein has a correlation time
                      of τβ ∼ 100 s. Moreover, we show that its
                      temperature-dependent amplitude has a crossover at the
                      regular glass transition Tg = 320 K of hydrated elastin,
                      where the α relaxation of the protein obeys τα ∼ 100 s.
                      By contrast, we do not observe a protein dynamical
                      transition when water dynamics enters the experimental time
                      window at ∼240 K.},
      cin          = {JCNS-FRM-II / MLZ / JCNS-1},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-1-20110106},
      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},
      pubmed       = {pmid:32610976},
      UT           = {WOS:000546996600001},
      doi          = {10.1063/5.0011107},
      url          = {https://juser.fz-juelich.de/record/877757},
}