Related Experiment Video
Updated: Aug 25, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
A new structural state of myosin
1Department of Chemistry, Dartmouth College, Hanover, NH 03755, USA.
Abstract:
The mechanism by which motor proteins hydrolyze ATP and move along cytoskeletal filaments is still unknown. One approach to deciphering the mechanism is to correlate steps of ATP hydrolysis with structural states of the motors to determine the changes the motors undergo during the hydrolysis cycle. Unfortunately, available crystal structures represent only a few steps of the cycle and obtaining atomic structures that represent the motors bound to their filament has been difficult. Now, two new myosin crystal structures have been reported that show features expected for myosin motors bound in rigor to actin. The two new structures show changes at both the actin-binding surface and the active site that have not been observed previously.
Related Concept Videos
Overview of Myosin Structure and Function
Actin and Myosin in Muscle Contraction
Cross-bridge Cycle
The Sarcomere
Each myosin...
ATP Synthase: Structure
Excitation-Contraction Coupling in Skeletal Muscles
When an action potential...
