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• W3136644544 abstract "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." @default.
• W3136644544 created "2021-03-29" @default.
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• W3136644544 date "2021-03-24" @default.
• W3136644544 modified "2023-09-27" @default.
• W3136644544 title "Sequence of Events During Peptide Unbinding from RNase S: A Complete Experimental Description" @default.
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• W3136644544 hasPublicationYear "2021" @default.
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