title: The myosin power stroke.
abstract: Optical trapping technology now allows investigators in the motility field to measure the forces generated by single motor molecules. A handful of research groups have exploited this approach to further develop our understanding of the actin-based motor, myosin, an ATPase that is capable of converting chemical energy into mechanical work during a cyclical interaction with filamentous actin. In this regard, myosin-II from muscle is the most well-characterized myosin superfamily member. By combining the data obtained from optical trap assays with that from ensemble biochemical and mechanical assays, this review discusses the fundamental properties of the myosin-II power stroke and, perhaps more significantly, how these properties are governed by this molecule's atomic structure and the biochemical transitions that define its catalytic cycle.
authors.affiliation: Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA. matthew.tyska@yale.edu
authors.forename: Matthew J
authors.initials: MJ
authors.lastname: Tyska
authors.forename: David M
authors.initials: DM
authors.lastname: Warshaw
mesh_terms: D000818:Animals; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000502:physiology*; D009119:Muscle Contraction / Q000502:physiology*; D009218:Myosins / Q000737:chemistry* / Q000502:physiology*; D017433:Protein Structure, Secondary
chemical_list: D020409:Molecular Motor Proteins; D009218:Myosins