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：

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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。