[3][11] During this same year, Taylor attended the University of Chicago, where he began his graduate studies in Biophysics and discovered an interest to research the mechanism of mitosis.
[3] As a postdoctoral fellow, Taylor spent two years in the laboratory of Francis Schmitt at Massachusetts Institute of Technology, investigating the properties of neurofilament proteins with Peter Davison.
While not in the laboratory, Taylor worked a half-time position as a Louis Block Professor of Molecular Genetics and Cell Biology at the University of Chicago.
[14] Through the investigation of molecular motors, myosin with actin and kinesin with microtubules, Taylor was eager to discover the kinetic mechanism that dictated the structural changes responsible for force and motion.
[3] His work in the laboratory not only led to his discovery of tubulin, the protein subunit of microtubules, but it also developed the first kinetic model explaining how these molecular motors could convert chemical energy into mechanical force.
[14] He investigates molecular motors, myosin with actin and kinesin with microtubules, to discover the kinetic mechanism that dictates the structural changes responsible for force and motion.
[11] This led to his discovery of tubulin, the protein subunit of microtubules, and to the first kinetic model explaining how these molecular motors convert chemical energy into mechanical force in striated muscle.
Taylor and graduate student, Gary Borisy, discovered colchicine was indeed specific and its highest binding activity was presented in dividing cells, mitotic apparatus, cilia, sperm tails, and brain tissue.
Microtubules conduct the mitotic spindle, constitute the 9 + 2 assortment of filaments in the cilia and sperm tails, and participate in the majority of neuronal processes.
[8] Using sea urchin eggs, Taylor and Borisy directed another experiment to further demonstrate that the location of binding sites resides in the mitotic apparatus.
[12] In 1979, Taylor and his research partners demonstrated that the binding of myosin to actin, following the release of a phosphate, produced a significant reduction in free energy.
[20] Taylor and fellow corresponding authors, Yvonne S. Aratyn, Thomas E. Schaus, and Gary G. Borisy, published the “Intrinsic Dynamic Behavior of Fascin in Filopodia” in 2007.
Results of their study showed that bundling in filopodial filaments requires the dephosphorylation of fascin, which can also initiate high-affinity actin binding in the filopodia.
In order for filopodial filaments to form, the process depends on the phosphorylation or dephosphorylation cycles that serve as the primary indicators of fascin inactivity or activity.
[22] Even twelve years later, what continued to remain misunderstood were the varying degrees of thin filament activation between pre- or post-power stroke myosin.
In “Investigation into the mechanism of thin filament regulation by transient kinetics and equilibrium binding: Is there a conflict?”, Taylor, along with David H. Heely and Howard D. White conduct research and provide more clarity to the issue.
[23] Published on March 4, 1999, The University of Chicago Chronicle writes about the honoring of Taylor at the National Institutes of Health in Bethesda, Maryland, with a science symposium.