Mechanochemical disulfide reduction reveals imprints of noncovalent sulfur⋯oxygen chalcogen bonds in protein-inspired mimics in aqueous solution
Author:
Affiliation:
1. Lehrstuhl für Theoretische Chemie
2. Ruhr-Universität Bochum
3. 44780 Bochum
4. Germany
Abstract
Chalcogen bonds in proteins are found to impact on the mechanochemical reduction of disulfide bridges in aqueous environments.
Funder
Narodowe Centrum Nauki
Deutsche Forschungsgemeinschaft
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2020/CP/D0CP04026F
Reference44 articles.
1. Force-dependent chemical kinetics of disulfide bond reduction observed with single-molecule techniques
2. Single-Molecule Force Spectroscopy Measurements of Bond Elongation during a Bimolecular Reaction
3. Force-activated reactivity switch in a bimolecular chemical reaction
4. Kinetics of Thiol/Disulfide Exchange Correlate Weakly with the Restoring Force in the Disulfide Moiety
5. Atomistic Evidence of How Force Dynamically Regulates Thiol/Disulfide Exchange
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