The unit event of sliding of the chemo-mechanical enzyme composed of myosin and actin with regulatory proteins.
Various myosin-actin systems do not always show the same sliding behaviors. To make the situation clear, discussions are concentrated on the unit event of sliding of the chemo-mechanical enzyme composed of a single myosin head and a single actin filament with regulatory proteins. The popular idea of the one-to-one correspondence between the chemical state and the physical state or between the chemical reaction step and the physical conformational change is reexamined. It is likely that the sites and the modes of interaction between myosin head and actin filament during the ATP hydrolysis are more multiple and variable, and the input-output coupling in the chemo-mechanical enzyme is loose.
D000199:Actins / Q000737:chemistry* / Q000502:physiology*; D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000502:physiology*; D001665:Binding Sites; D004789:Enzyme Activation; D008954:Models, Biological; D008956:Models, Chemical; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000502:physiology*; D009038:Motion; D009119:Muscle Contraction / Q000502:physiology; D009218:Myosins / Q000737:chemistry* / Q000502:physiology*; D011485:Protein Binding
D000199:Actins; D020409:Molecular Motor Proteins; D000251:Adenosine Triphosphatases; D009218:Myosins