Actin and myosin based motile systems are involved in a wide array of cellular motile functions ranging from muscle contraction to organelle transport. In all of these systems the mechanism through which myosin is able to produce force and generate movement is still poorly understood at a molecular level. To study myosin’s enzymatic mechanism in a simple and defined system, we employ laser trapping techniques and in vitro motility assays. Currently, our research focuses on mutations in cardiac myosin and troponin C to determine the effect of specific amino acid substitutions on acto-myosin's mechanical and enzymatic properties.

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