肽与RNase S解结合过程中的事件顺序：完整的实验描述
Sequence of Events During Peptide Unbinding from RNase S: A Complete Experimental Description
摘要：
的光触发的解结合的本质上无序的S-肽从RNase S复合物的研究与瞬态红外光谱的帮助下，覆盖了广泛的时间尺度从100 ps到10 ms。为此，偶氮苯部分已连接到S-肽的方式，其螺旋度被破坏的光，从而启动其完全解结合。观察到事件的完整顺序，从S-肽的螺旋结构在20 ns时间尺度上展开开始，同时仍然处于S-蛋白的结合口袋中，300微秒后S-肽解结合，以及3 ms后S-蛋白的结构响应。关于S-肽动力学，结合机制可以被分类为诱导配合，而S蛋白的结构反应更好地描述为构象选择。
英文摘要：
The photo-triggered unbinding of the intrinsically disordered S-peptide from the RNase S complex is studied with the help of transient IR spectroscopy, covering a wide range of time scales from 100 ps to 10 ms. To that end, an azobenzene moiety has been linked to the S-peptide in a way that its helicity is disrupted by light, thereby initiating its complete unbinding. The full sequence of events is observed, starting from unfolding of the helical structure of the S-peptide on a 20 ns timescale while still being in the binding pocket of the S-protein, S-peptide unbinding after 300 microseconds, and the structural response of the S-protein after 3 ms. With regard to the S-peptide dynamics, the binding mechanism can be classified as an induced fit, while the structural response of the S-protein is better described as conformational selection.
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