Movement and force produced by a single myosin head

  • Molloy J
  • Burns J
  • Kendrick-Jones B
 et al. 
  • 130


    Mendeley users who have this article in their library.
  • 461


    Citations of this article.


Muscle contraction is driven by the cyclical interaction of myosin with actin, coupled to the breakdown of ATP. Studies of the interaction of filamentous myosin and of a double-headed proteolytic fragment, heavy meromyosin (HMM), with actin have demonstrated discrete mechanical events, arising from stochastic interaction of single myosin molecules with actin. Here we show, using an optical-tweezers transducer, that a single myosin subfragment-1 (S1), which is a single myosin head, can act as an independent generator of force and movement. Our analysis accounts for the broad distribution of displacement amplitudes observed, and indicates that the underlying movement (working stroke) produced by a single acto-S1 interaction is approximately 4 nm, considerably shorter than previous estimates but consistent with structural data. We measure the average force generated by S1 or HMM to be at least 1.7 pN under isometric conditions.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document


  • J. E. Molloy

  • J. E. Burns

  • B. Kendrick-Jones

  • R. T. Tregear

  • D. C S White

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free