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Time-resolved infrared studies of the unfolding of a light triggered beta-hairpin peptide

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Moroder,  Luis
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Rampp, M. S., Hofmann, S. M., Podewin, T., Hoffmann-Roeder, A., Moroder, L., & Zinth, W. (2018). Time-resolved infrared studies of the unfolding of a light triggered beta-hairpin peptide. Chemical Physics, 512, 116-121. doi:10.1016/j.chemphys.2018.02.003.


Cite as: https://hdl.handle.net/21.11116/0000-0002-FD08-9
Abstract
The light triggered unfolding reaction of the azobenzene peptide AzoTrpZip2 is investigated from 1 ps to 100 mu s. Absorption changes show that the unfolding is a multistep process with the initial breaking of the hydrogen bonds in the vicinity of the AMPP chromophore on the 1 ns time scale followed by the disappearance of the remaining interstrand hydrogen bonds of the native hairpin structure with a 1.9 mu s process. Subsequently, the hydrophobic core structure still stabilising a hairpin-like pattern rearranges in a 17 mu s process. The strong slowing down of this reaction at lower temperature points to a barrier height in the range of 60 kJ/mol. (C) 2018 Published by Elsevier B.V.