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@ARTICLE{Frontzek:279334,
      author       = {Frontzek, Anna and Paccou, Laurent and Guinet, Yannick and
                      Hédoux, Alain},
      title        = {{S}tudy of the phase transition in lysozyme crystals by
                      {R}aman spectroscopy},
      journal      = {Biochimica et biophysica acta / General subjects},
      volume       = {1860},
      number       = {2},
      issn         = {0304-4165},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2015-07349},
      pages        = {412 - 423},
      year         = {2016},
      abstract     = {BackgroundRecently, it has been revealed that tetragonal
                      lysozyme crystals show a phase transition at 307 K upon
                      heating. The underlying mechanisms of the phase transition
                      are still not fully understood. Here we focus on the study
                      of high-frequency vibrational modes arising from the protein
                      and their temperature evolution in the vicinity of Tph as
                      well as on the detailed study of crystalline water dynamics
                      near Tph.MethodsRaman experiments have been performed at
                      temperatures 295–323 K including Tph. The low-frequency
                      modes and the modes of fingerprint region, CH- and
                      OH-stretching regions have been analyzed.Results and
                      conclusionsIn spite of the absence of noticeable
                      rearrangements in protein structure, the high-frequency
                      vibrational modes of lysozyme located in the fingerprint
                      region have been found to exhibit the features of critical
                      dynamics near Tph. Pronounced changes in the dynamics of
                      α-helixes and Tyr residues exposed on the protein surface
                      point to the important role of H-bond rearrangements at the
                      phase transition. Additionally the study of temperature
                      evolution of OH-stretching modes has shown an increase in
                      distortions of tertahedral H-bond network of crystalline
                      water above Tph. These changes in water dynamics could play
                      a crucial role in the mechanisms of the phase
                      transition.General significanceThe present results shed
                      light on the mechanisms of the phase transition in lysozyme
                      crystals.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6215 - Soft Matter, Health and Life Sciences (POF3-621) /
                      6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6215 / G:(DE-HGF)POF3-6G15 /
                      G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000368746500008},
      doi          = {10.1016/j.bbagen.2015.10.020},
      url          = {https://juser.fz-juelich.de/record/279334},
}