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@ARTICLE{Deeg:22704,
      author       = {Deeg, A.A. and Schrader, T.E. and Strzalka, H. and Pfizer,
                      J. and Moroder, L. and Zinth, W.},
      title        = {{A}myloid-{L}ike {S}tructures {F}ormed by {A}zobenzene
                      {P}eptides: {L}ight-{T}riggered {D}isassembly},
      journal      = {Spectroscopy: An International Journal},
      volume       = {27},
      issn         = {0887-6703},
      address      = {Springfield, Or.},
      publisher    = {Aster Pub. Corp.},
      reportid     = {PreJuSER-22704},
      pages        = {387 - 391},
      year         = {2012},
      note         = {The work was supported by the German Science Foundation,
                      SFB 749, and the Munich Center of Integrated Protein
                      Science, CIPSM. The University of Zurich did not contribute
                      to this work.},
      abstract     = {The light-driven disassembly process of amyloid-like
                      structures formed by azobenzene model peptides is studied by
                      time-resolved mid-IR spectroscopy from nanoseconds to
                      minutes. The investigated peptide consists of two amino acid
                      strands connected by the azobenzene switch. The peptides
                      aggregate to amyloid-like structures when the azobenzene
                      chromophore is in the trans-conformation. Illumination,
                      resulting in a trans-to cis-isomerization of the azobenzene,
                      leads to disaggregation of the aggregated structures. After
                      optical excitation and isomerization of the azobenzene, one
                      finds absorption changes which recover to a large extent on
                      the time scale of few nanoseconds. These early absorption
                      transients are assigned to the relaxation of vibrational
                      excess energy (heat) or to structural rearrangements of
                      isomerized azobenzene and the aggregated surroundings. It is
                      only on the time scale of minutes that spectral signatures
                      appear which are characteristic for the disassembly of the
                      aggregated structure.},
      keywords     = {J (WoSType)},
      cin          = {ICS-1 / JCNS (München) ; Jülich Centre for Neutron
                      Science JCNS (München) ; JCNS-FRM-II / JCNS-1},
      ddc          = {530},
      cid          = {I:(DE-Juel1)ICS-1-20110106 /
                      I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung (FUEK505) / 544 - In-house Research
                      with PNI (POF2-544)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-HGF)POF2-544},
      experiment   = {EXP:(DE-MLZ)External-20140101},
      shelfmark    = {Biochemical Research Methods / Spectroscopy},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000306505500016},
      doi          = {10.1155/2012/108959},
      url          = {https://juser.fz-juelich.de/record/22704},
}