The major challenge of our current research is to understand the cell biology and the biophysics of ATP driven molecular motors. Our goal is to construct mathematical models to account for their action of mechanism. More than 40 genes of myosins are encoded in the human genome, most of them are expressed in non-muscle cell lines with plethora of cellular functions and binding partners that are yet to be discovered. We are studying the roles, functions, and kinetic adaptation of Myo19-an actin-based motor that transfer mitochondria in response to cellular stress. We are conducting interdisciplinary research to understand its cellular function in migration by KD and KO genetic background of Myo19, live cell imaging and structure-function studies to understand its enzymatic adaptation. Within this family of motors we are also investigating the unique enzymology of Myo1C splice isoforms and their roles in both cytoplasmatic and nuclear compartments, with focus on their active part in nucleolus assembly for rDNA gene transcripts.  We are also studying the enzymology utilizing kinetics and thermodynamics of SF1 of DNA helicases. In this aspect, we are using RecBCD, a DNA helicase from E.coli essential for DSB repair, to understand how nucleotides binding manifest its unique extreme fast ATPase cycle and processive and high velocity DNA unwinding activities. We have revealed that this is enabled by novel mechanism of ATP auxiliary ATP binding sites that were not discovered before which assist to increase the flow and the local concentration of ATP to drive the enzyme extraordinary abilities in DNA unwinding. Understanding such mechanism is highly important to all other ATP driven molecular motors which still hold many unknowns open question mechanistically.  We aim to utilized are inside structure function to develop new drugs targeting human molecular motors.