Structural and functional investigations of novel kinesin assemblies: deciphering intersubunit communication in asymmetric motors

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A defining characteristic of life is movement. From our ability to walk down the street, to the distribution of individual molecules within our cells, movement is a basic necessity and tiny protein machines known as "motor proteins" power most forms of it. One of the best-known families of motor proteins are kinesins. These motors convert the energy released from breaking chemical bonds in high-energy molecules like ATP into mechanical force in order to move along protein tracks in cells. In the process, they transport various cargoes to their required destinations in the cell. Recent efforts in nanotechnology development have focused on kinesins and other motor proteins as a source of inspiration for building and powering nanoscale devices. A major goal of Dr. Allingham's research is to understand the aspects of kinesin motor design that confer their motile properties in order to facilitate rapid development in this area. The specific focus of studies currently underway in Dr. Allingham's laboratory involve deciphering the mechanism by which novel forms of kinesin from a variety of different organisms are able to coordinate the conversion of chemical energy into controlled movement. By determining the three-dimensional structures of these kinesins, observing their movement, and studying the effects of mutations on these parameters, Dr. Allingham's group hopes to gain insight into this mechanism, which could revolutionize our understanding of how motors carry out their various vital functions in cells and how these functions are regulated at different times and in different cell types. Such studies will also provide opportunities for graduate students to obtain multidisciplinary training in advanced research methods and allow them to make significant contributions to our understanding fundamental scientific questions.