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@ARTICLE{Fitter:29288,
      author       = {Fitter, J.},
      title        = {{A} measure of conformational entropy change during thermal
                      protein unfolding using neutron spectroscopy},
      journal      = {Biophysical journal},
      volume       = {84},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-29288},
      pages        = {3924 - 3930},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Thermal unfolding of proteins at high temperatures is
                      caused by a strong increase of the entropy change which
                      lowers Gibbs free energy change of the unfolding transition
                      (DeltaG(unf) = DeltaH - TDeltaS). The main contributions to
                      entropy are the conformational entropy of the polypeptide
                      chain itself and ordering of water molecules around
                      hydrophobic side chains of the protein. To elucidate the
                      role of conformational entropy upon thermal unfolding in
                      more detail, conformational dynamics in the time regime of
                      picoseconds was investigated with neutron spectroscopy.
                      Confined internal structural fluctuations were analyzed for
                      a-amylase in the folded and the unfolded state as a function
                      of temperature. A strong difference in structural
                      fluctuations between the folded and the unfolded state was
                      observed at 30 degreesC, which increased even more with
                      rising temperatures. A simple analytical model was used to
                      quantify the differences of the conformational space
                      explored by the observed protein dynamics for the folded and
                      unfolded state. Conformational entropy changes, calculated
                      on the basis of the applied model, show a significant
                      increase upon heating. In contrast to indirect estimates,
                      which proposed a temperature independent conformational
                      entropy change, the measurements presented here,
                      demonstrated that the conformational entropy change
                      increases with rising temperature and therefore contributes
                      to thermal unfolding.},
      keywords     = {J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000183129800038},
      url          = {https://juser.fz-juelich.de/record/29288},
}