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@ARTICLE{Abyzov:169187,
      author       = {Abyzov, Anton and Mandelkow, Eckhard and Zweckstetter,
                      Markus and Rezaei-Ghaleh, Nasrollah},
      title        = {{F}ast {M}otions {D}ominate {D}ynamics of {I}ntrinsically
                      {D}isordered {T}au {P}rotein at {H}igh {T}emperatures.},
      journal      = {Chemistry - a European journal},
      volume       = {29},
      number       = {17},
      issn         = {0947-6539},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {DZNE-2023-00066},
      pages        = {e202203493},
      year         = {2023},
      abstract     = {Reorientational dynamics of intrinsically disordered
                      proteins (IDPs) contain multiple motions often clustered
                      around three motional modes: ultrafast librational motions
                      of amide groups, fast local backbone conformational
                      fluctuations and slow chain segmental motions. This dynamic
                      picture is mainly based on 15 N NMR relaxation studies of
                      IDPs at relatively low temperatures where the amide-water
                      proton exchange rates are sufficiently small. Less is known,
                      however, about the dynamics of IDPs at more physiological
                      temperatures. Here, we investigate protein dynamics in a
                      441-residue long IDP, tau protein, in the temperature range
                      from 0-25 °C, using 15 N NMR relaxation rates and spectral
                      density analysis. While at these temperatures relaxation
                      rates are still better described in terms of amide group
                      librational motions, local backbone dynamics and chain
                      segmental motions, the temperature-dependent trend of
                      spectral densities suggests that the timescales of fast
                      backbone conformational fluctuations and slower chain
                      segmental motions might become inseparable at higher
                      temperatures. Our data demonstrate the remarkable dynamic
                      plasticity of this prototypical IDP and highlight the need
                      for dynamic studies of IDPs at multiple temperatures.},
      keywords     = {Temperature / Protein Conformation / tau Proteins /
                      Magnetic Resonance Spectroscopy / Intrinsically Disordered
                      Proteins: chemistry / Amides / tau Proteins (NLM Chemicals)
                      / Intrinsically disordered protein (Other) / NMR relaxation
                      (Other) / protein dynamics (Other) / spectral density
                      analysis (Other) / tau protein (Other) / Intrinsically
                      Disordered Proteins (NLM Chemicals) / Amides (NLM
                      Chemicals)},
      cin          = {AG Mandelkow 1 / AG Zweckstetter},
      ddc          = {540},
      cid          = {I:(DE-2719)1013014 / I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36579699},
      doi          = {10.1002/chem.202203493},
      url          = {https://pub.dzne.de/record/169187},
}