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@ARTICLE{Ameseder:847922,
      author       = {Ameseder, Felix and Radulescu, Aurel and Holderer, Olaf and
                      Falus, Peter and Richter, Dieter and Stadler, Andreas M.},
      title        = {{R}elevance of {I}nternal {F}riction and {S}tructural
                      {C}onstraints for the {D}ynamics of {D}enatured {B}ovine
                      {S}erum {A}lbumin},
      journal      = {The journal of physical chemistry letters},
      volume       = {9},
      number       = {10},
      issn         = {1948-7185},
      address      = {Washington, DC},
      publisher    = {ACS},
      reportid     = {FZJ-2018-03243},
      pages        = {2469 - 2473},
      year         = {2018},
      abstract     = {A general property of disordered proteins is their
                      structural expansion that results in a high molecular
                      flexibility. The structure and dynamics of bovine serum
                      albumin (BSA) denatured by guanidinium hydrochloride (GndCl)
                      were investigated using small-angle neutron scattering
                      (SANS) and neutron spin–echo spectroscopy (NSE). SANS
                      experiments demonstrated the relevance of intrachain
                      interactions for structural expansion. Using NSE
                      experiments, we observed a high internal flexibility of
                      denatured BSA in addition to center-of-mass diffusion
                      detected by dynamic light scattering. Internal motions
                      measured by NSE were described using concepts based on
                      polymer theory. The contribution of residue-solvent friction
                      was accounted for using the Zimm model including internal
                      friction (ZIF). Disulfide bonds forming loops of amino acids
                      of the peptide backbone have a major impact on internal
                      dynamics that can be interpreted with a reduced set of Zimm
                      modes.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1 /
                      JCNS-2},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106},
      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)KWS2-20140101 / EXP:(DE-MLZ)J-NSE-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29688725},
      UT           = {WOS:000432756600004},
      doi          = {10.1021/acs.jpclett.8b00825},
      url          = {https://juser.fz-juelich.de/record/847922},
}