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Cell Motil Cytoskeleton. 2002 Jan;51(1):1-15.

The myosin power stroke.

Author information

  • 1Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA. matthew.tyska@yale.edu

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.

Copyright 2002 Wiley-Liss, Inc.

PMID:
11810692
[PubMed - indexed for MEDLINE]
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