The elementary process in the actomyosin energy transduction system.
The sliding distance of an actin filament induced by a myosin head during one ATP hydrolysis cycle was determined by measuring minimum length of actin filaments moving on myosin-coated glass surface as fast as long ones and the ATPase rate during sliding. The results indicate that the sliding distance is greater than 100nm, suggesting that the mechanical reaction can occur many times during one chemical (ATP hydrolysis) cycle.
Harada
Y
Y
Department of Biophysical Engineering, Faculty of Engineering Science, Osaka University, Japan.
Yanagida
T
T
D000199:Actins / Q000648:ultrastructure; D000205:Actomyosin / Q000502:physiology*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D004734:Energy Metabolism / Q000502:physiology*; D008854:Microscopy, Electron; D008856:Microscopy, Fluorescence; D008956:Models, Chemical; D009132:Muscles / Q000378:metabolism / Q000502:physiology; D009218:Myosins / Q000648:ultrastructure; D014741:Video Recording
D000199:Actins; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D009218:Myosins