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@ARTICLE{Schrader:20194,
      author       = {Schrader, T.E. and Cordes, T. and Schreier, W.J. and
                      Koller, F.O. and Dong, S.-L. and Moroder, L. and Zinth, W.},
      title        = {{F}olding and {U}nfolding of {L}ight {T}riggered
                      beta-{H}airpin {M}odel {P}eptides},
      journal      = {The journal of physical chemistry / B},
      volume       = {115},
      issn         = {1520-6106},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PreJuSER-20194},
      pages        = {5219 - 5226},
      year         = {2011},
      note         = {The authors thank Alexander Milbradt, Christian Renner, and
                      Markus Loweneck for synthesis of the molecules and NMR
                      analysis, and Ulrike Kusebauch for helpful discussions.
                      Financial support from the Deutsche Forschungsgemeinschaft
                      (SFB 533 Projects A8, B9, and SFB 749, project A5) is highly
                      acknowledged. This work was also supported through the
                      DFG-Cluster of Excellence Munich-Centre for Advanced
                      Photonics. The authors thank Shaul Mukamel for many helpful
                      discussions on light triggered peptides.},
      abstract     = {Ultrafast spectroscopy in the visible and mid-infrared is
                      used to study the reaction dynamics of two light-triggered
                      model peptides containing an azobenzene derivative as a
                      switching element. One model peptide, the AzoTrpZip2, forms
                      a β-hairpin structure in the cis form of the chromophore.
                      This peptide is compared to the core structure consisting of
                      the chromophore and the two flanking amino acid residues,
                      used as a minimal model. This combination of experiments
                      performed in different spectral ranges on peptides of
                      different sizes allows for improved insight into light
                      triggered reaction dynamics. The kinetics observed for the
                      core structure are directly connected to the switching
                      process of the chromophore and are finished on the 10 ps
                      time scale. The trans-to-cis reaction of AzoTrpZip2, leading
                      to the formation of the β-hairpin structure involves
                      ultrafast processes on the 100 ps time scale, which are
                      directly related to the relaxation of the strain between the
                      isomerized molecular switch and the two peptide strands.
                      IR-signatures characteristic for changes in interstrand
                      interactions are absent on the <1 ns time scale. Thus
                      folding into the β-hairpin structure occurs on a much
                      longer time scale. In the cis-to-trans unfolding reaction,
                      all IR signatures related to changes in interstrand
                      interactions occur within 1 ns, in a time range where
                      visible spectroscopy reveals the final decay of the
                      intramolecular strain. Apparently unfolding of AzoTrpZip2 is
                      to a large extent a fast, driven process.},
      keywords     = {Amino Acid Sequence / Azo Compounds: chemistry / Inverted
                      Repeat Sequences / Peptides: chemistry / Protein Folding /
                      Protein Structure, Secondary / Protein Unfolding /
                      Spectrophotometry, Infrared / Azo Compounds (NLM Chemicals)
                      / Peptides (NLM Chemicals) / azobenzene (NLM Chemicals) / 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 / Großgeräte für die Forschung
                      mit Photonen, Neutronen und Ionen (PNI)},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK415},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      shelfmark    = {Chemistry, Physical},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:21175125},
      UT           = {WOS:000290127100018},
      doi          = {10.1021/jp107683d},
      url          = {https://juser.fz-juelich.de/record/20194},
}