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

Rampp, Michael S.; Hofmann, Stefan M.; Podewin, Tom; Hoffmann-Röder, Anja; Moroder, Luis; Zinth, Wolfgang (2018): Time-resolved infrared studies of the unfolding of a light triggered beta-hairpin peptide. In: Chemical Physics, Vol. 512: pp. 116-121

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.

• Item Type: Journal article
• Faculties: Chemistry and Pharmacy > Department of Chemistry
• Research Centers: Center for Integrated Protein Science Munich (CIPSM)
• Subjects: 500 Science > 540 Chemistry
• ISSN: 0301-0104
• Language: English