Video imaging of walking myosin V by high-speed atomic force microscopy

Nature. 2010 Nov 4;468(7320):72-6. doi: 10.1038/nature09450. Epub 2010 Oct 10.


The dynamic behaviour of myosin V molecules translocating along actin filaments has been mainly studied by optical microscopy. The processive hand-over-hand movement coupled with hydrolysis of adenosine triphosphate was thereby demonstrated. However, the protein molecules themselves are invisible in the observations and have therefore been visualized by electron microscopy in the stationary states. The concomitant assessment of structure and dynamics has been unfeasible, a situation prevailing throughout biological research. Here we directly visualize myosin V molecules walking along actin tracks, using high-speed atomic force microscopy. The high-resolution movies not only provide corroborative 'visual evidence' for previously speculated or demonstrated molecular behaviours, including lever-arm swing, but also reveal more detailed behaviours of the molecules, leading to a comprehensive understanding of the motor mechanism. Our direct and dynamic high-resolution visualization is a powerful new approach to studying the structure and dynamics of biomolecules in action.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / chemistry
  • Actins / metabolism
  • Actins / ultrastructure
  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / metabolism
  • Animals
  • Biotinylation
  • Chickens
  • Immobilized Proteins / chemistry
  • Immobilized Proteins / metabolism
  • Immobilized Proteins / ultrastructure
  • Microscopy, Atomic Force / methods*
  • Movement*
  • Myosin Type V / chemistry
  • Myosin Type V / metabolism*
  • Myosin Type V / ultrastructure*
  • Protein Conformation
  • Protein Unfolding
  • Time Factors
  • Video Recording*


  • Actins
  • Immobilized Proteins
  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Myosin Type V