Sequence of Events during Peptide Unbinding from RNase S: A Complete Experimental Description
نویسندگان
چکیده
The phototriggered unbinding of the intrinsically disordered S-peptide from RNase S complex is studied with help transient IR spectroscopy, covering a wide range time scales 100 ps to 10 ms. To that end, an azobenzene moiety has been linked in way its helicity disrupted by light, thereby initiating complete unbinding. full sequence events observed, starting unfolding helical structure on 20 ns scale while still being binding pocket S-protein, after 300 μs, and structural response S-protein 3 With regard dynamics, mechanism can be classified as induced fit, better described conformational selection.
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ژورنال
عنوان ژورنال: Journal of Physical Chemistry Letters
سال: 2021
ISSN: ['1948-7185']
DOI: https://doi.org/10.1021/acs.jpclett.1c01155