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@ARTICLE{Mckel:872747,
      author       = {Möckel, Christina and Kubiak, Jakub and Schillinger,
                      Oliver and Kühnemuth, Ralf and Della Corte, Dennis and
                      Schröder, Gunnar F. and Willbold, Dieter and Strodel,
                      Birgit and Seidel, Claus A. M. and Neudecker, Philipp},
      title        = {{I}ntegrated {NMR}, {F}luorescence, and {M}olecular
                      {D}ynamics {B}enchmark {S}tudy of {P}rotein {M}echanics and
                      {H}ydrodynamics},
      journal      = {The journal of physical chemistry / B B, Condensed matter,
                      materials, surfaces, interfaces $\&$ biophysical},
      volume       = {123},
      number       = {7},
      issn         = {1520-5207},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {FZJ-2020-00225},
      pages        = {1453 - 1480},
      year         = {2019},
      abstract     = {Understanding the function of a protein requires not only
                      knowledge of its tertiary structure but also an
                      understanding of its conformational dynamics. Nuclear
                      magnetic resonance (NMR) spectroscopy, polarization-resolved
                      fluorescence spectroscopy and molecular dynamics (MD)
                      simulations are powerful methods to provide detailed insight
                      into protein dynamics on multiple time scales by monitoring
                      global rotational diffusion and local flexibility (order
                      parameters) that are sensitive to inter- and intramolecular
                      interactions, respectively. We present an integrated
                      approach where data from these techniques are analyzed and
                      interpreted within a joint theoretical description of
                      depolarization and diffusion, demonstrating their conceptual
                      similarities. This integrated approach is then applied to
                      the autophagy-related protein GABARAP in its cytosolic form,
                      elucidating its dynamics on the pico- to nanosecond time
                      scale and its rotational and translational diffusion for
                      protein concentrations spanning 9 orders of magnitude. We
                      compare the dynamics of GABARAP as monitored by 15N spin
                      relaxation of the backbone amide groups, fluorescence
                      anisotropy decays and fluorescence correlation spectroscopy
                      of side chains labeled with BODIPY FL, and molecular movies
                      of the protein from MD simulations. The recovered parameters
                      agree very well between the distinct techniques if the
                      different measurement conditions (probe localization, sample
                      concentration) are taken into account. Moreover, we propose
                      a method that compares the order parameters of the backbone
                      and side chains to identify potential hinges for
                      large-scale, functionally relevant intradomain motions, such
                      as residues 27/28 at the interface between the two
                      subdomains of GABARAP. In conclusion, the integrated concept
                      of cross-fertilizing techniques presented here is
                      fundamental to obtaining a comprehensive quantitative
                      picture of multiscale protein dynamics and solvation. The
                      possibility to employ these validated techniques under
                      cellular conditions and combine them with fluorescence
                      imaging opens up the perspective of studying the functional
                      dynamics of GABARAP or other proteins in live cells.},
      cin          = {ICS-6 / JARA-HPC},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-6-20110106 / $I:(DE-82)080012_20140620$},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      IHRS-BioSoft - International Helmholtz Research School of
                      Biophysics and Soft Matter (IHRS-BioSoft-20061101) /
                      Structural dynamics of murine guanylate binding proteins,
                      their dimerization and interaction with lipid bilayers
                      $(jics6a_20180501)$},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-Juel1)IHRS-BioSoft-20061101 /
                      $G:(DE-Juel1)jics6a_20180501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30525615},
      UT           = {WOS:000459836700001},
      doi          = {10.1021/acs.jpcb.8b08903},
      url          = {https://juser.fz-juelich.de/record/872747},
}