I have logged 1470+ hours of tutoring students in biochemistry from across the globe online.

My research group uses several biophysical tools including transient state kinetics, isothermal titration calorimetry, X-ray crystallography, and light microscopy to study and understand necessary biological processes. Specifically, our central aim is to characterize the mechanism of energy transduction in kinesin and myosin superfamily motor proteins and elucidate how microtubules and actin filaments (respectively) stimulate their ATPase activity. My past research has focused on elucidating the mechanism of unconventional kinesin motors from the kinesin-5 (BimC/Eg5) and kinesin-10 (chromokinesin/NOD) families as well as characterizing non-muscle myosin-2 from Dictyostelium discoideum. Toward the end of my postdoctoral research and continuing as an independent investigator at Indiana University, I developed an innovative strategy to control the activity of kinesin motor proteins through substituting a single residue in the active site that rendered the enzyme sensitive to divalent cation (i.e. Mg2+ inhibited the motor, but Mn2+ rescued its normal activity). I have since tested this metal switch technology in non-muscle myosin-2 and have corroborated the structural link between switch 1 closing coupled to weakening the motor’s affinity for the filament. I have assembled a diverse research team, consisting of two graduate students, one research technician and two undergraduate researchers, and have established high-level collaborations within and outside Indiana University.NSF Investigator-Initiated Research Project (MCB-Molecular Biophysics) AwardIndiana University Faculty Research Support Program (FRSP) – External Resubmission AwardIndiana University Trustees Teaching AwardIndiana University Faculty Research Support Program (FRSP) Award

During my postdoctoral research, in collaboration with R. Scott Hawley at Stowers Institute for Medical Research, we investigated the high-resolution structure and enzymology of the NOD catalytic domain, a nonmotile kinesin-10 that localizes along chromosome arms and functions in the segregation of achiasmate chromosomes during meiosis. During this study, I established a fruitful and ongoing collaboration with Charles Sindelar at Lawrence Berkeley National Laboratory (now at Yale) to resolve a cryo-EM reconstruction of the nucleotide-free MT-NOD complex. In addition to work on NOD, we were able to characterize the detailed thermodynamics of nucleotide interaction with kinesin using isothermal titration calorimetry (ITC) methodologies, which represented my first senior author publication.Ruth L. Kirschstein National Research Service Award

During my dissertation research, we collaborated with Andreas Hoenger’s group at EMBL-Heidelberg (now at University of Colorado) to investigate the role of the C-termini of tubulin in modulating the binding of kinesin-1/conventional kinesin to microtubules. My doctoral dissertation research focused on the characterization of the monomeric Eg5 ATPase mechanism in the absence and presence of microtubules. These studies revealed that Eg5 remains tightly associated with the microtubule during most of the ATPase cycle, thus adapting the motor for its function within the mitotic spindle. In addition, our research provided mechanistic insight into how a prototype small molecule called monastrol acts to inhibit the ATPase mechanism of Eg5 motors.