Physical-Chemical Basis of the Contractile Mechanism

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Force is developed in muscle contraction by myosin molecule pulling actin filaments during shortening. The details of this process have been difficult to establish because of the rapid and unsynchronized nature of the many changes taking place during the relative sliding of the filaments. Our work is focused on the structural changes that are thought to be occurring in the head region of myosin during this interaction. The introduction of molecular biological techniques in recent years has permitted us to modify the polypeptide structure of myosin in such a way that reporter groups can be more readily introduced into the molecule. These groups can be fluorescent probes for spectroscopic studies, or electron dense probes for direct visualization by electron microscopy. These methods should provide new information about the dynamics of myosin crossbridge movement during ATP hydrolysis and actin binding, both in individual molecules and in muscle fibers during muscle contraction.