Sean Quinn

Kinesins are remarkable microtubule-based molecular motors in that they couple nucleotide hydrolysis to movement at millisecond or faster time scales! Single-molecule microscopy and stopped-flow kinetics experiments can provide the rates of different transitions within a kinesin’s stepping-cycle but cannot always provide a complete picture of how each motor domain behaves throughout a processive run. My research aims to determine how heterodimerization of kinesins, particularly kinesin-2, impacts the mechanochemical properties of its two motor domains. Addressing this question using modeling will allow us to gain an appreciation for why heterodimeric kinesins evolved and their significance in the cell. In addition, I am also fascinated by the roles of kinesins and other related molecular motors in neurological diseases.