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@ARTICLE{Stadler:283547,
      author       = {Stadler, Andreas and Knieps-Grünhagen, Esther and Bocola,
                      Marco and Lohstroh, Wiebke and Zamponi, Michaela and Krauss,
                      Ulrich},
      title        = {{P}hotoactivation {R}educes {S}ide-{C}hain {D}ynamics of a
                      {LOV} {P}hotoreceptor},
      journal      = {Biophysical journal},
      volume       = {110},
      number       = {5},
      issn         = {0006-3495},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2016-01863},
      pages        = {1064 - 1074},
      year         = {2016},
      abstract     = {We used neutron-scattering experiments to probe the
                      conformational dynamics of the light, oxygen, voltage (LOV)
                      photoreceptor PpSB1-LOV from Pseudomonas putida in both the
                      dark and light states. Global protein diffusion and internal
                      macromolecular dynamics were measured using incoherent
                      neutron time-of-flight and backscattering spectroscopy on
                      the picosecond to nanosecond timescales. Global protein
                      diffusion of PpSB1-LOV is not influenced by photoactivation.
                      Observation-time-dependent global diffusion coefficients
                      were found, which converge on the nanosecond timescale
                      toward diffusion coefficients determined by dynamic light
                      scattering. Mean-square displacements of localized internal
                      motions and effective force constants, <k′>, describing
                      the resilience of the proteins were determined on the
                      respective timescales. Photoactivation significantly
                      modifies the flexibility and the resilience of PpSB1-LOV. On
                      the fast, picosecond timescale, small changes in the
                      mean-square displacement and <k′> are observed, which are
                      enhanced on the slower, nanosecond timescale.
                      Photoactivation results in a slightly larger resilience of
                      the photoreceptor on the fast, picosecond timescale, whereas
                      in the nanosecond range, a significantly less resilient
                      structure of the light-state protein is observed. For a
                      residue-resolved interpretation of the experimental
                      neutron-scattering data, we analyzed molecular dynamics
                      simulations of the PpSB1-LOV X-ray structure. Based on these
                      data, it is tempting to speculate that light-induced changes
                      in the protein result in altered side-chain mobility mostly
                      for residues on the protruding Jα helix and on the LOV-LOV
                      dimer interface. Our results provide strong experimental
                      evidence that side-chain dynamics play a crucial role in
                      photoactivation and signaling of PpSB1-LOV via modulation of
                      conformational entropy.},
      cin          = {ICS-1 / Neutronenstreuung ; JCNS-1 / JCNS (München) ;
                      Jülich Centre for Neutron Science JCNS (München) ;
                      JCNS-FRM-II / IMET},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)IMET-20090612},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)SPHERES-20140101 /
                      EXP:(DE-MLZ)TOF-TOF-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000371850000015},
      pubmed       = {pmid:26958884},
      doi          = {10.1016/j.bpj.2016.01.021},
      url          = {https://juser.fz-juelich.de/record/283547},
}