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Intrinsic Dynamics of Protein–Peptide Unbinding


Jankovic, Brankica; Bozovic, Olga; Hamm, Peter (2021). Intrinsic Dynamics of Protein–Peptide Unbinding. Biochemistry, 60(22):1755-1763.

Abstract

The dynamics of peptide–protein binding and unbinding of a variant of the RNase S system has been investigated. To initiate the process, a photoswitchable azobenzene moiety has been covalently linked to the S-peptide, thereby switching its binding affinity to the S-protein. Transient fluorescence quenching was measured with the help of a time-resolved fluorometer, which has been specifically designed for these experiments and is based on inexpensive light-emitting diodes and laser diodes only. One mutant shows on–off behavior with no specific binding detectable in one of the states of the photoswitch. Unbinding is faster by at least 2 orders of magnitude, compared to that of other variants of the RNase S system. We conclude that unbinding is essentially barrier-less in that case, revealing the intrinsic dynamics of the unbinding event, which occurs on a time scale of a few hundred microseconds in a strongly stretched-exponential manner.

Abstract

The dynamics of peptide–protein binding and unbinding of a variant of the RNase S system has been investigated. To initiate the process, a photoswitchable azobenzene moiety has been covalently linked to the S-peptide, thereby switching its binding affinity to the S-protein. Transient fluorescence quenching was measured with the help of a time-resolved fluorometer, which has been specifically designed for these experiments and is based on inexpensive light-emitting diodes and laser diodes only. One mutant shows on–off behavior with no specific binding detectable in one of the states of the photoswitch. Unbinding is faster by at least 2 orders of magnitude, compared to that of other variants of the RNase S system. We conclude that unbinding is essentially barrier-less in that case, revealing the intrinsic dynamics of the unbinding event, which occurs on a time scale of a few hundred microseconds in a strongly stretched-exponential manner.

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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:Life Sciences > Biochemistry
Uncontrolled Keywords:Biochemistry
Language:English
Date:8 June 2021
Deposited On:20 Oct 2021 12:52
Last Modified:26 Mar 2024 02:39
Publisher:American Chemical Society (ACS)
ISSN:0006-2960
OA Status:Green
Publisher DOI:https://doi.org/10.1021/acs.biochem.1c00262
Project Information:
  • : FunderSNSF
  • : Grant ID200020B_188694
  • : Project TitleUltrafast Vibrational Spectroscopy of Allosteric Proteins (Extension)
  • Content: Accepted Version