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@ARTICLE{Grimaldo:187418,
      author       = {Grimaldo, Marco and Roosen-Runge, Felix and Hennig, Marcus
                      and Zanini, Fabio and Zhang, Fajun and Jalarvo, Niina and
                      Zamponi, Michaela and Schreiber, Frank and Seydel, Tilo},
      title        = {{H}ierarchical molecular dynamics of bovine serum albumin
                      in concentrated aqueous solution below and above thermal
                      denaturation},
      journal      = {Physical chemistry, chemical physics},
      volume       = {17},
      number       = {6},
      issn         = {1463-9084},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {FZJ-2015-01087},
      pages        = {4645 - 4655},
      year         = {2015},
      abstract     = {The dynamics of proteins in solution is a complex and
                      hierarchical process, affected by the aqueous environment as
                      well as temperature. We present a comprehensive study on
                      nanosecond time and nanometer length scales below, at, and
                      above the denaturation temperature Td. Our experimental data
                      evidence dynamical processes in protein solutions on three
                      distinct time scales. We suggest a consistent physical
                      picture of hierarchical protein dynamics: (i) self-diffusion
                      of the entire protein molecule is confirmed to agree with
                      colloid theory for all temperatures where the protein is in
                      its native conformational state. At higher temperatures T >
                      Td, the self-diffusion is strongly obstructed by
                      cross-linking or entanglement. (ii) The amplitude of
                      backbone fluctuations grows with increasing T, and a
                      transition in its dynamics is observed above Td. (iii) The
                      number of mobile side-chains increases sharply at Td while
                      their average dynamics exhibits only little variations. The
                      combination of quasi-elastic neutron scattering and the
                      presented analytical framework provides a detailed
                      microscopic picture of the protein molecular dynamics in
                      solution, thereby reflecting the changes of macroscopic
                      properties such as cluster formation and gelation.},
      cin          = {ICS-1 / Neutronenstreuung ; JCNS-1 / Jülich Centre for
                      Neutron Science JCNS (JCNS) ; JCNS / JCNS (München) ;
                      Jülich Centre for Neutron Science JCNS (München) ;
                      JCNS-FRM-II},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-SNS-20110128 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)External-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000349005900077},
      pubmed       = {pmid:25587698},
      doi          = {10.1039/C4CP04944F},
      url          = {https://juser.fz-juelich.de/record/187418},
}