Kinesins are motor proteins that are involved in critical cellular processes such as chromosome segregation (NOD) and embryonic development (Costal 2). The first structure of a kinesin motor domain was solved by Jon Kull during his graduate work with Professors Robert Fletterick and Ronald Vale at UCSF in 1996 (Kull et al. Nature, 1996). In the Kull Lab, we have been interested in the structural study of molecular motors and the relation between structure and enzymatic activity. We aim to gain a thorough understanding of the detailed mechanism of motor protein based force generation. Each crystal structure of a motor protein represents a static snapshot of a highly dynamic process. By solving structures in different nucleotide states, or of highly divergent family members, it is possible to build up a clearer picture of the overall dynamics of the process. Previous work by our laboratory has demonstrated that kinesin and myosin share a common motor core, as well as a great deal of similarity in their catalytic mechanisms and initial pathway of conformational change. These similarities can be used to form hypotheses as to the nature of the missing states. Future experimental work aimed at targeting the function of motors involved in specific cellular functions could lead to the development of therapeutics against a number of diseases and pathogens.