SFB 969 TP A02: Untersuchung der Strukturbildung von Proteinen mittels zeitaufgelöster Infrarot-Spektroskopie
- FB Chemie
|(2016): Site-specific dynamics of β-sheet peptides with DPro-Gly turns probed by laser-excited temperature-jump infrared spectroscopy ChemPhysChem. 2016, 17(9), pp. 1273-1280. ISSN 1439-4235. eISSN 1439-7641. Available under: doi: 10.1002/cphc.201501089||
Site-specific dynamics of β-sheet peptides with DPro-Gly turns probed by laser-excited temperature-jump infrared spectroscopy
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.
|Period:||01.01.2012 – 31.12.2015|