When I worked at the National Institutes of Health, my team was concerned with the molecular mechanism of human movement and studied the interaction of myosin crossbridges with actin filaments in muscle fibers. After our discovery of weakly-binding crossbridge interactions in muscle fibers in 1982, my group focused on learning how crossbridge interactions with actin in the fiber relate to the interaction of myosin with actin in solution. Our effort initially was directed towards understanding the weakly-binding interaction we had discovered, but subsequently we also studied the unique aspects of the strongly-binding interaction that distinguish it from the weakly-binding interaction. This enabled us to define the key property that distinguishes the two types of interaction.
We subsequently developed methods for modifying myosin crossbridges within a single muscle fiber in order to learn more about which parts of the myosin molecule are important in the weakly-binding to strongly-binding conformational change that accompanies ATP hydrolysis and is essential for force generation. These studies were never completed as I instead became more interested in fulfilling my lifelong desire to live in Israel.
Updated Apr 20, 2010