000020194 001__ 20194
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000020194 0247_ $$2DOI$$a10.1021/jp107683d
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000020194 084__ $$2WoS$$aChemistry, Physical
000020194 1001_ $$0P:(DE-Juel1)138266$$aSchrader, T.E.$$b0$$uFZJ
000020194 245__ $$aFolding and Unfolding of Light Triggered beta-Hairpin Model Peptides
000020194 260__ $$aWashington, DC$$bSoc.$$c2011
000020194 300__ $$a5219 - 5226
000020194 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000020194 440_0 $$03694$$aJournal of Physical Chemistry B$$v115$$x1520-6106$$y18
000020194 500__ $$aThe 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.
000020194 520__ $$aUltrafast spectroscopy in the visible and mid-infrared is used to study the reaction dynamics of two light-triggered model peptides containing an azobenzene derivative as a switching element. One model peptide, the AzoTrpZip2, forms a β-hairpin structure in the cis form of the chromophore. This peptide is compared to the core structure consisting of the chromophore and the two flanking amino acid residues, used as a minimal model. This combination of experiments performed in different spectral ranges on peptides of different sizes allows for improved insight into light triggered reaction dynamics. The kinetics observed for the core structure are directly connected to the switching process of the chromophore and are finished on the 10 ps time scale. The trans-to-cis reaction of AzoTrpZip2, leading to the formation of the β-hairpin structure involves ultrafast processes on the 100 ps time scale, which are directly related to the relaxation of the strain between the isomerized molecular switch and the two peptide strands. IR-signatures characteristic for changes in interstrand interactions are absent on the <1 ns time scale. Thus folding into the β-hairpin structure occurs on a much longer time scale. In the cis-to-trans unfolding reaction, all IR signatures related to changes in interstrand interactions occur within 1 ns, in a time range where visible spectroscopy reveals the final decay of the intramolecular strain. Apparently unfolding of AzoTrpZip2 is to a large extent a fast, driven process.
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000020194 588__ $$aDataset connected to Web of Science, Pubmed
000020194 650_2 $$2MeSH$$aAmino Acid Sequence
000020194 650_2 $$2MeSH$$aAzo Compounds: chemistry
000020194 650_2 $$2MeSH$$aInverted Repeat Sequences
000020194 650_2 $$2MeSH$$aPeptides: chemistry
000020194 650_2 $$2MeSH$$aProtein Folding
000020194 650_2 $$2MeSH$$aProtein Structure, Secondary
000020194 650_2 $$2MeSH$$aProtein Unfolding
000020194 650_2 $$2MeSH$$aSpectrophotometry, Infrared
000020194 650_7 $$00$$2NLM Chemicals$$aAzo Compounds
000020194 650_7 $$00$$2NLM Chemicals$$aPeptides
000020194 650_7 $$0103-33-3$$2NLM Chemicals$$aazobenzene
000020194 650_7 $$2WoSType$$aJ
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000020194 7001_ $$0P:(DE-HGF)0$$aCordes, T.$$b1
000020194 7001_ $$0P:(DE-HGF)0$$aSchreier, W.J.$$b2
000020194 7001_ $$0P:(DE-HGF)0$$aKoller, F.O.$$b3
000020194 7001_ $$0P:(DE-HGF)0$$aDong, S.-L.$$b4
000020194 7001_ $$0P:(DE-HGF)0$$aMoroder, L.$$b5
000020194 7001_ $$0P:(DE-HGF)0$$aZinth, W.$$b6
000020194 773__ $$0PERI:(DE-600)2006039-7$$a10.1021/jp107683d$$gVol. 115, p. 5219 - 5226$$p5219 - 5226$$q115<5219 - 5226$$tThe @journal of physical chemistry <Washington, DC> / B$$v115$$x1520-6106$$y2011
000020194 8567_ $$uhttp://dx.doi.org/10.1021/jp107683d
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