Long-Range Charge Reorganization as an Allosteric Control Signal in Proteins.
Journal
Journal of the American Chemical Society
ISSN: 1520-5126
Titre abrégé: J Am Chem Soc
Pays: United States
ID NLM: 7503056
Informations de publication
Date de publication:
02 12 2020
02 12 2020
Historique:
pubmed:
20
11
2020
medline:
20
4
2021
entrez:
19
11
2020
Statut:
ppublish
Résumé
A new mechanism of allostery in proteins, based on charge rather than structure, is reported. We demonstrate that dynamic redistribution of charge within a protein can control its function and affect its interaction with a binding partner. In particular, the association of an antibody with its target protein antigen is studied. Dynamic charge shifting within the antibody during its interaction with the antigen is enabled by its binding to a metallic surface that serves as a source for electrons. The kinetics of antibody-antigen association are enhanced when charge redistribution is allowed, even though charge injection happens at a position far from the antigen binding site. This observation points to
Identifiants
pubmed: 33211484
doi: 10.1021/jacs.0c10105
pmc: PMC7735699
doi:
Substances chimiques
Amino Acids
0
Antibodies, Immobilized
0
Sulfhydryl Compounds
0
Gold
7440-57-5
Endopeptidase Clp
EC 3.4.21.92
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
20456-20462Références
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