A model for the chemomechanical coupling of myosin-V molecular motors.
Journal
RSC advances
ISSN: 2046-2069
Titre abrégé: RSC Adv
Pays: England
ID NLM: 101581657
Informations de publication
Date de publication:
23 Aug 2019
23 Aug 2019
Historique:
received:
04
07
2019
accepted:
13
08
2019
entrez:
9
5
2022
pubmed:
27
8
2019
medline:
27
8
2019
Statut:
epublish
Résumé
Herein, a model for the chemomechanical coupling of dimeric myosin-V motors is presented. Based on this model and the proposal that the rate constants of the ATPase activity of the two heads are independent of an external force in a range smaller than the stall force, we analytically studied the dynamics of the motor, such as the stepping ratio, dwell time between two mechanical steps, and velocity, under varying force and ATP concentrations. The theoretical results well reproduce the diverse available single-molecule experimental data. In particular, the experimental data showing that at a low ATP concentration, the dwell time and velocity have less force dependency than at a high ATP concentration is explained quantitatively. Moreover, the dependency of the chemomechanical coupling ratio on the force and ATP concentration was studied.
Identifiants
pubmed: 35528596
doi: 10.1039/c9ra05072h
pii: c9ra05072h
pmc: PMC9070430
doi:
Types de publication
Journal Article
Langues
eng
Pagination
26734-26747Informations de copyright
This journal is © The Royal Society of Chemistry.
Déclaration de conflit d'intérêts
No conflict of interest exists.
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