Under the hood of nanomotor proteins:  

My lab studies how these molecular machines work.  The kinesin family of motor proteins are essential for the life of all eukaryotic cells; anything that moves inside a cell, is moved by a motor protein along a cytoskeletal highway network.  In particular, the Kinesin-5 family is required for mitosis in all dividing cells and also plays a special role in (nondividing) neurons, particularly dendrites.  Unlike bipedal walker, Kinesin-1, Kinesin-5 forms a homotetramer that can crosslink, bundle, and slide microtubules to build higher order cellular machinery, such as the mitotic spindle.

GIF based on a crystal structure (3HQD) we solved in-house.

The kinesin-5 motor domain is a highly allosteric system of converting free energy of ATP hydrolysis to mechanical work (illustrated by this GIF);  how does this system work?  Small next-gen anti-cancer molecules that have been designed to inhibit Kinesin-5, and thereby block cell division, are used in my lab as probes to help understand many different aspects of how these enzymes work.  Many of these inhibitors are allosteric, and we would like to know how they bind and impact the distal active site to halt motility.  Second, we would like to understand how these compounds can elicit very different outcomes with Kinesin-5 despite binding to the same allosteric binding site.  Third, we seek to clarify how Kinesin-5 is designed to cooperate with other kinesin motors which then assemble large-scale molecular structures such as the mitotic spindle and dendritic spines and connections.