English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

A discrete-state model of the F1-ATPase molecular motor is developed whichdescribes not only the dependences of the rotation and ATP consumption rates onthe chemical concentrations of ATP, ADP, and inorganic phosphate, but also onmechanical control parameters such as the friction coefficient and the externaltorque. The dependence on these mechanical parameters is given to thediscrete-state model by fitting its transition rates to the continuous-anglemodel of P. Gaspard and E. Gerritsma [J. Theor. Biol. 247 (2007) 672-686]. Thisdiscrete-state model describes the behavior of the F1 motor in the regime oftight coupling between mechanical motion and chemical reaction. In this way,kinetic and thermodynamic properties of the F1 motor are obtained such as theMichaelis-Menten dependence of the rotation and ATP consumption rates on ATPconcentration and its extension in the presence of ADP and Pi, theirdependences on friction and external torque, as well as the chemical andmechanical thermodynamic efficiencies.

Discrete- versus continuous-state descriptions of the F1-ATPase molecular motor