@article{Popp2016Sites-33889,
  year={2016},
  doi={10.1002/cphc.201501089},
  title={Site-specific dynamics of β-sheet peptides with <sup>D</sup>Pro-Gly turns probed by laser-excited temperature-jump infrared spectroscopy},
  number={9},
  volume={17},
  issn={1439-4235},
  journal={ChemPhysChem},
  pages={1273--1280},
  author={Popp, Alexander and Scheerer, David and Chi, Heng and Keiderling, Timothy A. and Hauser, Karin}
}

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    <dc:creator>Scheerer, David</dc:creator>
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    <dcterms:title>Site-specific dynamics of β-sheet peptides with &lt;sup&gt;D&lt;/sup&gt;Pro-Gly turns probed by laser-excited temperature-jump infrared spectroscopy</dcterms:title>
    <dc:language>eng</dc:language>
    <dc:contributor>Popp, Alexander</dc:contributor>
    <dc:creator>Hauser, Karin</dc:creator>
    <dc:contributor>Scheerer, David</dc:contributor>
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    <dc:creator>Popp, Alexander</dc:creator>
    <dc:creator>Keiderling, Timothy A.</dc:creator>
    <dc:contributor>Chi, Heng</dc:contributor>
    <dc:contributor>Hauser, Karin</dc:contributor>
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    <dc:contributor>Keiderling, Timothy A.</dc:contributor>
    <dc:creator>Chi, Heng</dc:creator>
    <dcterms:abstract xml:lang="eng">Turn residues as well as side-chain interactions play an important role for the folding of ß-sheets. We investigated the conformational dynamics of a three-stranded ß-sheet peptide (&lt;sup&gt;D&lt;/sup&gt;P&lt;sup&gt;D&lt;/sup&gt;P) and a two-stranded ß-hairpin (WVYY-&lt;sup&gt;D&lt;/sup&gt;P) by time-resolved temperature-jump infrared spectroscopy. Both peptide sequences contain &lt;sup&gt;D&lt;/sup&gt;Pro-Gly residues that favor a tight ß-turn. The three-stranded ß-sheet (Ac-VFITS&lt;sup&gt;D&lt;/sup&gt;PGKTYTEV&lt;sup&gt;D&lt;/sup&gt;PGOKILQ-NH&lt;sub&gt;2&lt;/sub&gt;) is stabilized by the turn sequences, whereas the ß-hairpin (SWTVE&lt;sup&gt;D&lt;/sup&gt;PGKYTYK-NH&lt;sub&gt;2&lt;/sub&gt;) folding is assisted both by the turn sequence and by hydrophobic cross-strand interactions. Relaxation times after the T-jump were monitored as a function of temperature and occur on a sub-microsecond time scale, &lt;sup&gt;D&lt;/sup&gt;P&lt;sup&gt;D&lt;/sup&gt;P being faster than WVYY-&lt;sup&gt;D&lt;/sup&gt;P. The Xxx-&lt;sup&gt;D&lt;/sup&gt;Pro tertiary amide provides a detectable IR band allowing us to site-specifically probe the dynamics. The relative importance of the turn versus the intra-strand stability in ß-sheet formation is discussed.</dcterms:abstract>
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