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Site-specific dynamics of β-sheet peptides with <sup>D</sup>Pro-Gly turns probed by laser-excited temperature-jump infrared spectroscopy

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

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POPP, 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. 17(9), pp. 1273-1280. ISSN 1439-4235. eISSN 1439-7641. Available under: doi: 10.1002/cphc.201501089

@article{Popp2016Sites-33889, title={Site-specific dynamics of β-sheet peptides with DPro-Gly turns probed by laser-excited temperature-jump infrared spectroscopy}, year={2016}, doi={10.1002/cphc.201501089}, 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} }

2016-05-12T09:31:14Z 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 (<sup>D</sup>P<sup>D</sup>P) and a two-stranded ß-hairpin (WVYY-<sup>D</sup>P) by time-resolved temperature-jump infrared spectroscopy. Both peptide sequences contain <sup>D</sup>Pro-Gly residues that favor a tight ß-turn. The three-stranded ß-sheet (Ac-VFITS<sup>D</sup>PGKTYTEV<sup>D</sup>PGOKILQ-NH<sub>2</sub>) is stabilized by the turn sequences, whereas the ß-hairpin (SWTVE<sup>D</sup>PGKYTYK-NH<sub>2</sub>) 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, <sup>D</sup>P<sup>D</sup>P being faster than WVYY-<sup>D</sup>P. The Xxx-<sup>D</sup>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. Hauser, Karin Hauser, Karin Keiderling, Timothy A. 2016 Scheerer, David Popp, Alexander eng Chi, Heng Site-specific dynamics of β-sheet peptides with <sup>D</sup>Pro-Gly turns probed by laser-excited temperature-jump infrared spectroscopy Scheerer, David Popp, Alexander Keiderling, Timothy A. Chi, Heng 2016-05-12T09:31:14Z

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