Related Experiment Video
Updated: Oct 2, 2026

Dissecting Mechanoenzymatic Properties of Processive Myosins with Ultrafast Force-Clamp Spectroscopy
Published on: July 1, 2021
The myosin power stroke
Matthew J Tyska1, David M Warshaw
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.
Related Concept Videos
Actin and Myosin in Muscle Contraction
Cross-bridge Cycle
Excitation-Contraction Coupling in Skeletal Muscles
When an action potential...
Overview of Myosin Structure and Function
ATP Synthase: Mechanism
ATP Synthase: Structure

