Insights into the mechanisms of myosin and kinesin molecular motors from the single-molecule unbinding force measurements

Sergey Mikhailenko, Yusuke Oguchi, Shin'ichi Ishiwata

Research output: Contribution to journalArticle

6 Citations (Scopus)


In cells, ATP (adenosine triphosphate)-driven motor proteins, both cytoskeletal and nucleic acid-based, operate on their corresponding 'tracks', that is, actin, microtubules or nucleic acids, by converting the chemical energy of ATP hydrolysis into mechanical work. During each mechanochemical cycle, a motor proceeds via several nucleotide states, characterized by different affinities for the 'track' filament and different nucleotide (ATP or ADP) binding kinetics, which is crucial for a motor to efficiently perform its cellular functions. The measurements of the rupture force between the motor and the track by applying external loads to the individual motor-substrate bonds in various nucleotide states have proved to be an important tool to obtain valuable insights into the mechanism of the motors' performance.We review the application of this technique to various linear molecular motors, both processive and nonprocessive, giving special attention to the importance of the experimental geometry.

Original languageEnglish
JournalJournal of the Royal Society Interface
Issue numberSUPPL. 3
Publication statusPublished - 2010 Jun 6



  • Kinesin
  • Molecular motors
  • Myosin
  • Optical tweezers
  • Single molecules
  • Unbinding force

ASJC Scopus subject areas

  • Biophysics
  • Biotechnology
  • Bioengineering
  • Biomedical Engineering
  • Biomaterials
  • Biochemistry
  • Medicine(all)

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