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@ARTICLE{Haris:908298,
      author       = {Haris, Luman and Biehl, Ralf and Dulle, Martin and
                      Radulescu, Aurel and Holderer, Olaf and Hoffmann, Ingo and
                      Stadler, Andreas M.},
      title        = {{V}ariation of {S}tructural and {D}ynamical {F}lexibility
                      of {M}yelin {B}asic {P}rotein in {R}esponse to {G}uanidinium
                      {C}hloride},
      journal      = {International journal of molecular sciences},
      volume       = {23},
      number       = {13},
      issn         = {1422-0067},
      address      = {Basel},
      publisher    = {Molecular Diversity Preservation International},
      reportid     = {FZJ-2022-02518},
      pages        = {6969 -},
      year         = {2022},
      abstract     = {Myelin basic protein (MBP) is intrinsically disordered in
                      solution and is considered as a conformationally flexible
                      biomacromolecule. Here, we present a study on perturbation
                      of MBP structure and dynamics by the denaturant guanidinium
                      chloride (GndCl) using small-angle scattering and neutron
                      spin–echo spectroscopy (NSE). A concentration of 0.2 M
                      GndCl causes charge screening in MBP resulting in a compact,
                      but still disordered protein conformation, while GndCl
                      concentrations above 1 M lead to structural expansion and
                      swelling of MBP. NSE data of MBP were analyzed using the
                      Zimm model with internal friction (ZIF) and normal mode (NM)
                      analysis. A significant contribution of internal friction
                      was found in compact states of MBP that approaches a
                      non-vanishing internal friction relaxation time of
                      approximately 40 ns at high GndCl concentrations. NM
                      analysis demonstrates that the relaxation rates of internal
                      modes of MBP remain unaffected by GndCl, while structural
                      expansion due to GndCl results in increased amplitudes of
                      internal motions. Within the model of the Brownian
                      oscillator our observations can be rationalized by a loss of
                      friction within the protein due to structural expansion. Our
                      study highlights the intimate coupling of structural and
                      dynamical plasticity of MBP, and its fundamental difference
                      to the behavior of ideal polymers in solution.},
      cin          = {JCNS-FRM-II / JCNS-1 / JCNS-4 / IBI-8 / MLZ},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-4-20201012 /
                      I:(DE-Juel1)IBI-8-20200312 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4) / 632 - Materials – Quantum, Complex and
                      Functional Materials (POF4-632)},
      pid          = {G:(DE-HGF)POF4-6G4 / G:(DE-HGF)POF4-632},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 / EXP:(DE-MLZ)J-NSE-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {35805997},
      UT           = {WOS:000823509300001},
      doi          = {10.3390/ijms23136969},
      url          = {https://juser.fz-juelich.de/record/908298},
}