Molecular motors convert chemical energy into mechanical force. Muscle contraction and many other dynamic processes within cells are driven by myosin motors that produce mechanical force along actin filaments. Determination of the interaction between myosin and actin at the molecular level is necessary for understanding the mechanism of force production. Therefore, we plan to study this interaction at the molecular level by the reconstruction of acto-myosin complexes imaged in vitrified ice by cryo electron microscopy and by a determination of the binding affinities during the enzymatic cycle. Through the comparison of the interaction of different naturally occuring myosins with actin, we do hope to elucidate the detailed mechanism of force production and to understand how changes in actin interaction affect the physiological properties of different myosins. These informations may eventually allow the construction of nanomachines with defined properties.
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