Related Experiment Video
Updated: Aug 13, 2026

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Model for kinetics of myosin-V molecular motors
Ping Xie1, Shuo-Xing Dou, Peng-Ye Wang
1Laboratory of Soft Matter Physics, Beijing National Laboratory for Condensed Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100080, China. pxie@aphy.iphy.ac.cn
Abstract:
A hand-over-hand model is presented for the processive movement of myosin-V based on previous biochemical experimental results and structural observations of nucleotide-dependent conformational changes of single-headed myosins. The model shows that the ADP-release rate of the trailing head is much higher than that of the leading head, thus giving a 1:1 mechanochemical coupling for the processive movement of the motor. It explains well the previous finding that some 36-nm steps consist of two substeps, while other 36-nm steps consist of no substeps. Using the model, the calculated kinetic behaviors of myosin-V such as the main and intermediate dwell time distributions, the load dependence of the average main and intermediate dwell time and the load dependence of occurrence frequency of the intermediate state under various nucleotide conditions show good quantitative agreement with previous experimental results.
Related Concept Videos
Overview of Myosin Structure and Function
Introduction to Enzyme Kinetics
The experimenter can then plot the initial reaction rate or velocity (Vo) of a given trial against the substrate concentration ([S]) to obtain a graph of the reaction properties. For many enzymatic reactions involving a...
ATP Synthase: Mechanism
The Movement of Organelles and Vesicles
Actin and Myosin in Muscle Contraction
Enzyme Kinetics
Scientists typically study enzyme kinetics with a fixed amount of enzyme in the controlled environment of a test tube. When more reactant, or substrate, is...

