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@ARTICLE{Katava:827265,
      author       = {Katava, Marina and Maccarini, Marco and Villain, Guillaume
                      and Paciaroni, Alessandro and Sztucki, Michael and Ivanova,
                      Oxana and Madern, Dominique and Sterpone, Fabio},
      title        = {{T}hermal activation of ‘allosteric-like’ large-scale
                      motions in a eukaryotic {L}actate {D}ehydrogenase},
      journal      = {Scientific reports},
      volume       = {7},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2017-01459},
      pages        = {41092 -},
      year         = {2017},
      abstract     = {Conformational changes occurring during the enzymatic
                      turnover are essential for the regulation of protein
                      functionality. Individuating the protein regions involved in
                      these changes and the associated mechanical modes is still a
                      challenge at both experimental and theoretical levels. We
                      present here a detailed investigation of the thermal
                      activation of the functional modes and conformational
                      changes in a eukaryotic Lactate Dehydrogenase enzyme (LDH).
                      Neutron Spin Echo spectroscopy and Molecular Dynamics
                      simulations were used to uncover the characteristic length-
                      and timescales of the LDH nanoscale motions in the apo
                      state. The modes involving the catalytic loop and the mobile
                      region around the binding site are activated at room
                      temperature, and match the allosteric reorganisation of
                      bacterial LDHs. In a temperature window of about
                      15 degrees, these modes render the protein flexible enough
                      and capable of reorganising the active site toward reactive
                      configurations. On the other hand an excess of thermal
                      excitation leads to the distortion of the protein matrix
                      with a possible anti-catalytic effect. Thus, the temperature
                      activates eukaryotic LDHs via the same conformational
                      changes observed in the allosteric bacterial LDHs. Our
                      investigation provides an extended molecular picture of
                      eukaryotic LDH’s conformational landscape that enriches
                      the static view based on crystallographic studies alone.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {000},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)J-NSE-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000392465800001},
      doi          = {10.1038/srep41092},
      url          = {https://juser.fz-juelich.de/record/827265},
}