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"Time-resolved infrared studies of the unfolding of a light triggered β-hairpin peptide" M.S. Rampp, S.M. Hofmann, T. Podewin, A. Hoffmann-Röder, L. Moroder, W. ZinthChemPhys512(2018)116-121 Abstract: The light triggered unfolding reaction of the azobenzene peptide AzoTrpZip2 is investigated from 1 ps to 100 µs. 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 µs process. Subsequently, the hydrophobic core structure still stabilising a hairpin-like pattern rearranges in a 17 µs process. The strong slowing down of this reaction at lower temperature points to a barrier height in the range of 60 kJ/mol. BMO authors (in alphabetic order): Stefan Hofmann Michael Rampp Wolfgang Zinth  WWW-Version |
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Letzte Änderung: 2016-09-14 13:34
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