Research Overview

Why study muscle and cell motility?

The movements of our limbs, the beating of our heart and the peristalsis of our gut are all powered by our muscles. Using electron microscopy (EM), we can investigate the molecular basis of these movements. Muscles contract by interaction of filaments of the motor protein, myosin, with actin filaments, causing them to move past each other. Recent, revolutionary advances in cryo-EM enable us to peer into myosin structure on the near-atomic level, providing exciting new insights into its molecular function. Some cardiac and skeletal muscle diseases are a direct result of mutations in myosin. Understanding the atomic structure of myosin is revealing how these mutations cause disease and how recently FDA-approved therapeutic drugs work, making this an exciting time to be studying myosin structure and function. Below is an example where we resolved the structure of myosin in its inhibited state to 4.3 Å resolution (Yang et al., Nature 2020; 588:521-5).