Ensemble velocity of non-processive molecular motors with multiple chemical states

@article{Vilfan2014EnsembleVO,
  title={Ensemble velocity of non-processive molecular motors with multiple chemical states},
  author={Andrej Vilfan},
  journal={Interface Focus},
  year={2014},
  volume={4}
}
  • A. Vilfan
  • Published 27 September 2014
  • Physics
  • Interface Focus
We study the ensemble velocity of non-processive motor proteins, described with multiple chemical states. In particular, we discuss the velocity as a function of ATP concentration. Even a simple model which neglects the strain dependence of transition rates, reverse transition rates and nonlinearities in the elasticity can show interesting functional dependencies, which deviate significantly from the frequently assumed Michaelis–Menten form. We discuss how the order of events in the duty cycle… 
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References

SHOWING 1-10 OF 74 REFERENCES

Molecular motors: a theorist's perspective.

This review focuses on discrete kinetic and stochastic models that yield predictions for the mean velocity, V(F, [ATP], ...), and other observables as a function of an imposed load force F, the ATP concentration, and other variables.

Porters versus rowers: a unified stochastic model of motor proteins

A general phenomenological theory for chemical to mechanical energy transduction by motor enzymes which is based on the classical "tight-coupling" mechanism is presented, which explains in a unified way many results of recent in vitro motility assays.

Motor protein mechanics: a stochastic model with minimal mechanochemical coupling.

Molecular model of muscle contraction.

  • T. Duke
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
The model indicates that when large numbers of myosin molecules act collectively, their chemical cycles can be synchronized, and that this leads to stepwise motion of the thin filament.

Mechanoenzymes under superstall and large assisting loads reveal structural features

It transpires that the large-load performance is determined by the geometrical placement of the intermediate mechanochemical states of the enzymatic cycles relative to the associated transition states, and physical colocalization of biochemically distinct states generally implies large- load velocity saturation.

Simple mechanochemistry describes the dynamics of kinesin molecules

The simplest (N = 2)-state model with fixed load-distribution factors and kinetic rate constants concordant with stopped-flow experiments, accounts for the global (V, F, L, [ATP]) interdependence and, further, matches relative acceleration observed under assisting loads.

Twirling motion of actin filaments in gliding assays with nonprocessive Myosin motors.

Cooperativity of myosin molecules through strain-dependent chemistry.

  • T. Duke
  • Biology, Chemistry
    Philosophical transactions of the Royal Society of London. Series B, Biological sciences
  • 2000
Two aspects of cooperative action are discussed, in the context of a simple stochastic model, and if the lever swings through a large angle when phosphate is released, this leads to stepwise sliding of the filaments and suggests that the isometric condition is not a steady state.

Single kinesin molecules studied with a molecular force clamp

The kinesin cycle contains at least one load-dependent transition affecting the rate at which ATP molecules bind and subsequently commit to hydrolysis, and it is likely that at leastOne other load- dependent rate exists, affecting turnover number.

Kinesin hydrolyses one ATP per 8-nm step

Kinesin is a two-headed, ATP-dependent motor protein that moves along microtubules indiscrete steps of 8 nm. In vitro, single molecules produceprocessive movement, motors typically take ∼100steps…
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