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@ARTICLE{Parigi:137646,
      author       = {Parigi, Giacomo and Rezaei-Ghaleh, Nasrollah and Giachetti,
                      Andrea and Becker, Stefan and Fernandez, Claudio and
                      Blackledge, Martin and Griesinger, Christian and
                      Zweckstetter, Markus and Luchinat, Claudio},
      title        = {{L}ong-range correlated dynamics in intrinsically
                      disordered proteins.},
      journal      = {Journal of the American Chemical Society},
      volume       = {136},
      number       = {46},
      issn         = {0002-7863},
      address      = {Washington, DC},
      publisher    = {American Chemical Society},
      reportid     = {DZNE-2020-03968},
      pages        = {16201-16209},
      year         = {2014},
      abstract     = {Intrinsically disordered proteins (IDPs) are involved in a
                      wide variety of physiological and pathological processes and
                      are best described by ensembles of rapidly interconverting
                      conformers. Using fast field cycling relaxation measurements
                      we here show that the IDP α-synuclein as well as a variety
                      of other IDPs undergoes slow reorientations at time scales
                      comparable to folded proteins. The slow motions are not
                      perturbed by mutations in α-synuclein, which are related to
                      genetic forms of Parkinson's disease, and do not depend on
                      secondary and tertiary structural propensities.
                      Ensemble-based hydrodynamic calculations suggest that the
                      time scale of the underlying correlated motion is largely
                      determined by hydrodynamic coupling between locally rigid
                      segments. Our study indicates that long-range correlated
                      dynamics are an intrinsic property of IDPs and offers a
                      general physical mechanism of correlated motions in highly
                      flexible biomolecular systems.},
      keywords     = {Animals / Chemical Phenomena / Intrinsically Disordered
                      Proteins: chemistry / Intrinsically Disordered Proteins:
                      genetics / Intrinsically Disordered Proteins: metabolism /
                      Models, Molecular / Mutation / Protein Conformation /
                      Protons / Temperature / Water: chemistry / alpha-Synuclein:
                      chemistry / alpha-Synuclein: genetics / alpha-Synuclein:
                      metabolism / Intrinsically Disordered Proteins (NLM
                      Chemicals) / Protons (NLM Chemicals) / alpha-Synuclein (NLM
                      Chemicals) / Water (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {540},
      cid          = {I:(DE-2719)1410001},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25331250},
      doi          = {10.1021/ja506820r},
      url          = {https://pub.dzne.de/record/137646},
}