Molecular motors: Stretching the lever-arm theory

@article{Geeves2002MolecularMS,
  title={Molecular motors: Stretching the lever-arm theory},
  author={Michael A. Geeves},
  journal={Nature},
  year={2002},
  volume={415},
  pages={129-131}
}
  • M. Geeves
  • Published 10 January 2002
  • Biology
  • Nature
Motor proteins are essential to life: without them, all cellular transport would grind to a halt. New results on the size of steps taken by one family of motors, the myosins, will fuel the debate about how they move. 

A new model for myosin dimeric motors incorporating Brownian ratchet and powerstroke mechanisms

A new dimer model is introduced to describe the behavior of dimeric processive motor proteins in general and the results are compared with experimental data for two-headed processive motors.

Power-Stroke-Driven Muscle Contraction

To show that acto-myosin contraction can be propelled directly through a conformational change, we present in these lecture notes a review of a recently developed approach to muscle contraction where

An electromechanical model of myosin molecular motors.

  • T. Masuda
  • Biology
    Journal of theoretical biology
  • 2003

Conformational change of the actomyosin complex drives the multiple stepping movement

A theoretical model in which the refolding of the partially unfolded actomyosin complex and the movement of the myosin head along the actin filament are coupled is proposed, which quantitatively explains the single-molecular observation of the multiple stepping movement and is consistent with structural observations of the disorder in the actomyOSin-binding process.

Molecular dynamics simulation for the reversed power stroke motion of a myosin subfragment-1

...

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Here it is shown that myosin VI is also processive by using single molecule motility and optical trapping experiments, and takes much larger steps than expected, based on a simple lever-arm mechanism, for aMyosin with only one light chain in the lever- arm domain.

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