Kalen Z. Robeson

The paper re-examines the SRX state in myosin using mant-ATP displacement assays and finds no evidence of the SRX state in isolated myosin but detects two components in myofibrils, suggesting distinct myosin populations in thick filaments.

This study shows that the E525K β-myosin mutation reduces cardiomyocyte contraction without altering crossbridge cycling, through structural and computational analysis.

This study investigates how the E525K mutation in cardiac myosin affects its structure and function by analyzing conformational changes using cryo-EM and MD simulations.

The paper uses molecular dynamics simulations to show how conformational changes in loop 2 of myosin affect actomyosin association strength through electrostatic interactions.