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Many of linear molecular motors, such as myosins and kinesins, have two “feet” (traditionally called “heads” or “motor domains”) that bind to a motor-specific track and that each host a catalytic site for hydrolyzing ATP to power unidirectional movement along the track (, ; ; ; ; ; ; ). Some of the linear motors, such as conventional kinesin (; ; ; ; ), myosin V (; ; ), myosin VI (; ; ; ), and plant myosin XI (), are processive, in that a single motor molecule proceeds along a filamentous track for many ATPase cycles without detaching from the track. That the two feet never detach simultaneously from the track (or the ground in case of a human) is an important feature of “walking,” as opposed to “running” (). In addition, at least for myosin V and conventional kinesin which are known to be processive, convincing evidence exists that these motors throw their two feet forward alternately in a hand-over-hand fashion (, ; ; ; ), just as a human does.

Actin has been a major target for structural studies in biology since F. B. Straub discovered it in 1942. This is probably because actin is one of the most abundant proteins in the eukaryotic cell as well as a key player in many physiological events, ranging from genetics to motility.