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Sequence of Events during Peptide Unbinding from RNase S: A Complete Experimental Description


Jankovic, Brankica; Ruf, Jeannette; Zanobini, Claudio; Bozovic, Olga; Buhrke, David; Hamm, Peter (2021). Sequence of Events during Peptide Unbinding from RNase S: A Complete Experimental Description. Journal of Physical Chemistry Letters, 12(21):5201-5207.

Abstract

The phototriggered 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 time scale while still being in the binding pocket of the S-protein, S-peptide unbinding after 300 μs, 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.

Abstract

The phototriggered 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 time scale while still being in the binding pocket of the S-protein, S-peptide unbinding after 300 μs, 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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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Scopus Subject Areas:Physical Sciences > General Materials Science
Physical Sciences > Physical and Theoretical Chemistry
Uncontrolled Keywords:General Materials Science, Physical and Theoretical Chemistry
Language:English
Date:3 June 2021
Deposited On:20 Oct 2021 12:53
Last Modified:25 Feb 2024 02:45
Publisher:American Chemical Society (ACS)
ISSN:1948-7185
OA Status:Green
Publisher DOI:https://doi.org/10.1021/acs.jpclett.1c01155
Project Information:
  • : FunderSNSF
  • : Grant ID200020B_188694
  • : Project TitleUltrafast Vibrational Spectroscopy of Allosteric Proteins (Extension)
  • Content: Accepted Version