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@ARTICLE{Duy:51328,
      author       = {Duy, C. and Fitter, J.},
      title        = {{H}ow aggregation and conformational scrambling of unfolded
                      states govern fluorescence emission spectra},
      journal      = {Biophysical journal},
      volume       = {90},
      issn         = {0006-3495},
      address      = {New York, NY},
      publisher    = {Rockefeller Univ. Press},
      reportid     = {PreJuSER-51328},
      pages        = {3704 - 3711},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {In a case study on five homologous alpha-amylases we
                      analyzed the properties of unfolded states as obtained from
                      treatments with GndHCl and with elevated temperatures. In
                      particular the wavelength of the tryptophan fluorescence
                      emission peak (lambda(max)) is a valuable parameter to
                      characterize properties of the unfolded state. In all cases
                      with a typical red shift of the emission spectrum occurring
                      during structural unfolding we observed a larger magnitude
                      of this shift for GndHCl-induced unfolding as compared to
                      thermal unfolding. Although a quantitative relation between
                      aggregation and reduction of the unfolding induced red
                      shifts cannot be given, our data indicate that protein
                      aggregation contributes significantly to smaller magnitudes
                      of red shifts as observed during thermal unfolding. In
                      addition, other properties of the unfolded states, most
                      probable structural compactness or simply differences in the
                      conformational scrambling, also affect the magnitude of red
                      shifts. For the irreversible unfolding alpha-amylases
                      studied here, transition temperatures and magnitudes of red
                      shifts are strongly depending on heating rates. Lower
                      protein concentrations and smaller heating rates lead to
                      larger red shifts upon thermal unfolding, indicating that
                      under these conditions the protein aggregation is less
                      pronounced.},
      keywords     = {Dimerization / Multiprotein Complexes: analysis /
                      Multiprotein Complexes: chemistry / Protein Conformation /
                      Protein Denaturation / Protein Folding / Spectrometry,
                      Fluorescence: methods / Structure-Activity Relationship /
                      Temperature / alpha-Amylases: analysis / alpha-Amylases:
                      chemistry / Multiprotein Complexes (NLM Chemicals) /
                      alpha-Amylases (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:16500981},
      pmc          = {pmc:PMC1440751},
      UT           = {WOS:000236901400033},
      doi          = {10.1529/biophysj.105.078980},
      url          = {https://juser.fz-juelich.de/record/51328},
}