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Time-resolved infrared studies of the unfolding of a light triggered β-hairpin peptide
Chemical Physics ( IF 2.0 ) Pub Date : 2018-02-06 , DOI: 10.1016/j.chemphys.2018.02.003
Michael S. Rampp , Stefan M. Hofmann , Tom Podewin , Anja Hoffmann-Röder , Luis Moroder , Wolfgang Zinth

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.



中文翻译:

时间分辨的红外研究光触发的β-发夹肽的展开

从1 ps到100 µs研究了偶氮苯肽AzoTrpZip2的光触发解折叠反应。吸收变化表明,展开是一个多步过程,在1 ns的时间尺度上,AMPP发色团附近的氢键开始断裂,然后以1.9 µs的时间消失天然发夹结构的其余链间氢键。过程。随后,疏水核结构仍以17 µs的过程重新稳定了发夹状图案。在较低温度下该反应的强烈减慢表明势垒高度在60kJ / mol的范围内。

更新日期:2018-06-03
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