Publikation: Impact of β-turn sequence on β-hairpin dynamics studied with infrared-detected temperature jump
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2012
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Spectroscopy: An International Journal. 2012, 27, pp. 557-564. ISSN 0712-4813. Available under: doi: 10.1155/2012/102423
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Folding dynamics for β-structure loss and disordered structure gain were studied in a model β-hairpin peptide based on Cochran’s tryptophan zipper peptide Trpzip2, but with an altered Thr-Gly (TG) turn sequence, that is, SWTWETGKWTWK, using laser-induced temperature-jump (T-jump) kinetics with IR detection. As has been shown previously, the TG turn sequence reduces the thermodynamic β-hairpin stability as compared to the Asn-Gly sequence used in Trpzip2 (TZ2-NG). In this study, we found that the TG-turn slows down the overall relaxation dynamics as compared to TZ2-NG, which were studied at higher temperatures where the time constants show little difference between relaxation of the β-strand and the disordered conformation. These time constants become equivalent at lower temperatures for TZ2-TG than was seen for TZ2-NG. The correlation of thermodynamic stability and rates of relaxation suggests that the change from NG to TG turn results in a slowing of folding, lower kf, with less change of the unfolding rate, ku, assuming two state behavior at higher temperatures.
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POPP, Alexander, Ling WU, Timothy A. KEIDERLING, Karin HAUSER, 2012. Impact of β-turn sequence on β-hairpin dynamics studied with infrared-detected temperature jump. In: Spectroscopy: An International Journal. 2012, 27, pp. 557-564. ISSN 0712-4813. Available under: doi: 10.1155/2012/102423BibTex
@article{Popp2012Impac-22635,
year={2012},
doi={10.1155/2012/102423},
title={Impact of β-turn sequence on β-hairpin dynamics studied with infrared-detected temperature jump},
volume={27},
issn={0712-4813},
journal={Spectroscopy: An International Journal},
pages={557--564},
author={Popp, Alexander and Wu, Ling and Keiderling, Timothy A. and Hauser, Karin}
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<dcterms:abstract xml:lang="eng">Folding dynamics for β-structure loss and disordered structure gain were studied in a model β-hairpin peptide based on Cochran’s tryptophan zipper peptide Trpzip2, but with an altered Thr-Gly (TG) turn sequence, that is, SWTWETGKWTWK, using laser-induced temperature-jump (T-jump) kinetics with IR detection. As has been shown previously, the TG turn sequence reduces the thermodynamic β-hairpin stability as compared to the Asn-Gly sequence used in Trpzip2 (TZ2-NG). In this study, we found that the TG-turn slows down the overall relaxation dynamics as compared to TZ2-NG, which were studied at higher temperatures where the time constants show little difference between relaxation of the β-strand and the disordered conformation. These time constants become equivalent at lower temperatures for TZ2-TG than was seen for TZ2-NG. The correlation of thermodynamic stability and rates of relaxation suggests that the change from NG to TG turn results in a slowing of folding, lower k<sub>f</sub>, with less change of the unfolding rate, k<sub>u</sub>, assuming two state behavior at higher temperatures.</dcterms:abstract>
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