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Site-specific dynamics of β-sheet peptides with DPro-Gly turns probed by laser-excited temperature-jump infrared spectroscopy

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2016

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Chi, Heng
Keiderling, Timothy A.

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https://doi.org/10.1002/cphc.201501089
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SFB 969 TP A02: Untersuchung der Strukturbildung von Proteinen mittels zeitaufgelöster Infrarot-Spektroskopie
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ChemPhysChem. 2016, 17(9), pp. 1273-1280. ISSN 1439-4235. eISSN 1439-7641. Available under: doi: 10.1002/cphc.201501089

Zusammenfassung

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 (DPDP) and a two-stranded ß-hairpin (WVYY-DP) by time-resolved temperature-jump infrared spectroscopy. Both peptide sequences contain DPro-Gly residues that favor a tight ß-turn. The three-stranded ß-sheet (Ac-VFITSDPGKTYTEVDPGOKILQ-NH2) is stabilized by the turn sequences, whereas the ß-hairpin (SWTVEDPGKYTYK-NH2) 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, DPDP being faster than WVYY-DP. The Xxx-DPro 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.

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540 Chemie

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T -jump, b -sheet, infrared spectroscopy

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ISO 690POPP, Alexander, David SCHEERER, Heng CHI, Timothy A. KEIDERLING, Karin HAUSER, 2016. Site-specific dynamics of β-sheet peptides with DPro-Gly turns probed by laser-excited temperature-jump infrared spectroscopy. In: ChemPhysChem. 2016, 17(9), pp. 1273-1280. ISSN 1439-4235. eISSN 1439-7641. Available under: doi: 10.1002/cphc.201501089
BibTex
@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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    <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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