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@ARTICLE{Fischer:890360,
      author       = {Fischer, Jennifer and Radulescu, Aurel and Falus, Peter and
                      Richter, Dieter and Biehl, Ralf},
      title        = {{S}tructure and {D}ynamics of {R}ibonuclease {A} during
                      {T}hermal {U}nfolding: {T}he {F}ailure of the {Z}imm
                      {M}odel},
      journal      = {The journal of physical chemistry / B},
      volume       = {125},
      number       = {3},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2021-00905},
      pages        = {780 - 788},
      year         = {2021},
      abstract     = {Disordered regions as found in intrinsically disordered
                      proteins (IDP) or during protein folding define response
                      time to stimuli and protein folding times. Neutron spin-echo
                      spectroscopy is a powerful tool to directly access the
                      collective motions of the unfolded chain to enlighten the
                      physical origin of basic conformational relaxation. During
                      the thermal unfolding of native ribonuclease A, we examine
                      the structure and dynamics of the disordered state within a
                      two-state transition model using polymer models, including
                      internal friction, to describe the chain dynamics. The
                      presence of four disulfide bonds alters the disordered
                      configuration to a more compact configuration compared to a
                      Gaussian chain that is defined by the additional links, as
                      demonstrated by coarse-grained simulation. The dynamics of
                      the disordered chain is described by Zimm dynamics with
                      internal friction (ZIF) between neighboring amino acids.
                      Relaxation times are dominated by mode-independent internal
                      friction. Internal friction relaxation times show an
                      Arrhenius-like behavior with an activation energy of 33
                      kJ/mol. The Zimm dynamics is dominated by internal friction
                      and suggest that the characteristic motions correspond to
                      overdamped elastic modes similar to the motions observed for
                      folded proteins but within a pool of disordered
                      configurations spanning the configurational space. For IDP,
                      internal friction dominates while solvent friction and
                      hydrodynamic interactions are smaller corrections.},
      cin          = {JCNS-FRM-II / MLZ / JCNS-1 / JCNS-2 / JCNS-4},
      ddc          = {530},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)JCNS-2-20110106 /
                      I:(DE-Juel1)JCNS-4-20201012},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (FZJ)
                      (POF4-6G4)},
      pid          = {G:(DE-HGF)POF4-6G4},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101 /
                      EXP:(DE-H253)DORISIII(machine)-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {33470118},
      UT           = {WOS:000614308000009},
      doi          = {10.1021/acs.jpcb.0c09476},
      url          = {https://juser.fz-juelich.de/record/890360},
}