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

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.

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 Creators:
Rampp, Michael S.1, Author
Hofmann, Stefan M.1, Author
Podewin, Tom1, Author
Hoffmann-Roeder, Anja1, Author
Moroder, Luis2, Author           
Zinth, Wolfgang1, Author
Affiliations:
1external, ou_persistent22              
2Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565160              

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Free keywords: IR SPECTROSCOPY; ULTRAFAST SPECTROSCOPY; MOLECULAR-DYNAMICS; OPTICAL CONTROL; AZOBENZENE; JUMP; KINETICS; PHOTOISOMERIZATION; ISOMERIZATION; SWITCHChemistry; Physics;
 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.

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Language(s): eng - English
 Dates: 2018-022018
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Degree: -

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Title: Chemical Physics
  Other : Chem. Phys.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier B.V.
Pages: - Volume / Issue: 512 Sequence Number: - Start / End Page: 116 - 121 Identifier: ISSN: 0301-0104
CoNE: https://pure.mpg.de/cone/journals/resource/954925509371