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@ARTICLE{Ameseder:844243,
      author       = {Ameseder, Felix and Radulescu, Aurel and Khaneft, Marina
                      and Lohstroh, Wiebke and Stadler, Andreas M.},
      title        = {{H}omogeneous and heterogeneous dynamics in native and
                      denatured bovine serum albumin},
      journal      = {Physical chemistry, chemical physics},
      volume       = {20},
      number       = {7},
      issn         = {1463-9084},
      address      = {Cambridge},
      publisher    = {RSC Publ.},
      reportid     = {FZJ-2018-01684},
      pages        = {5128 - 5139},
      year         = {2018},
      abstract     = {A characteristic property of unfolded and disordered
                      proteins is their high molecular flexibility, which enables
                      the exploration of a large conformational space. We present
                      neutron scattering experiments on the dynamics of denatured
                      and native folded bovine serum albumin (BSA) in solution.
                      Global protein diffusion and internal macromolecular
                      dynamics were measured using quasielastic neutron
                      time-of-flight and backscattering spectroscopy on the
                      picosecond to nanosecond time- and Ångstrom length-scale.
                      Internal protein dynamics were analysed in a first approach
                      using stretched exponential functions. In denatured BSA
                      predominantly slow heterogeneous dynamics dominates the
                      observed macromolecular motions. Reduction of disulphide
                      bridges in denatured BSA does not significantly alter the
                      visible motions. In native folded BSA fast homogeneous
                      dynamics and slow heterogeneous dynamics were observed. In
                      an alternative data analysis approach, internal protein
                      dynamics was interpreted using the analytical model of the
                      overdamped Brownian oscillator, which allowed us to extract
                      mean square displacements of protein internal dynamics and
                      the fraction of hydrogen atoms participating in the observed
                      motions. Our results demonstrate that denaturation modifies
                      the physical nature of internal protein dynamics
                      significantly as compared to the native folded structure.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)SPHERES-20140101 /
                      EXP:(DE-MLZ)TOF-TOF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29392269},
      UT           = {WOS:000425107800053},
      doi          = {10.1039/C7CP08292D},
      url          = {https://juser.fz-juelich.de/record/844243},
}