Edwin W. Taylor

Edwin W. Taylor is an adjunct professor of cell and developmental biology at Northwestern University. He was elected to the National Academy of Sciences in 2001. Taylor received a BA in physics and chemistry from the University of Toronto in 1952; an MSc in physical chemistry from McMaster University in 1955, and a PhD in biophysics from the University of Chicago in 1957. In 2001 Taylor was elected to the National Academy of Sciences in Cellular and Developmental Biology and Biochemistry.

Taylor has made contributions to the way muscles contract and other related cytoskeletal research. His research described the first kinetic model of how molecular motors are able to change chemical energy to mechanical force. He uncovered several molecular cell motors, including some that help certain white blood cells to move. He also elucidated how actin and myosin create movement in non-muscle cells. who was a graduate student in Taylor's lab, discovered the protein that is the building block of microtubules, although the name of that protein, tubulin, was not coined until 1968. In 1967 Taylor found that the action of colchicine binding to cells could be modeled by a single kind of binding sites, perhaps showing that a unique target might exist. Taylor spends his summers in Woods Hole Research Center in Massachusetts.

Education In 1952, Taylor earned his Bachelor of Arts degree in Physics and Chemistry at the University of Toronto. He received a Master of Science degree from McMaster University in Physical Chemistry by 1955. 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. His Ph.D. dissertation focused on measuring the rates of mitotic processes. He was able to assess spindles and their rate of growth through the application of polarized light microscopy. By 1957, he acquired his Ph.D. in Biophysics from the University of Chicago.

Research Taylor focused a significant amount of his research on the molecular mechanisms regulating the movement of cells. particularly the chemical events involved in muscle contraction cycles.

In 1967, Borisy and Taylor published their work, “The Mechanism of Action of Colchicine. Binding of Colchincine-3H to Cellular Protein.” As these conditions reduce the colchicine-binding activity, results conclude the absence of the microtubules.

Once kinesin, a motor protein and anterograde transporter of vesicles in axons, was discovered, Taylor devoted his time to researching the kinetic mechanism. The limiting rate is governed by the rate that ADP in the hydrolysis cycle dissociates. Additionally, Taylor and Richard Lymn concluded in 1971 that actomyosin ATPase’s slow rate-limiting step could be attributed to the rate-limiting dissociation of the products, ADP, and phosphate from the enzyme. This led to the idea that actin could be a potential influence in the rate of product dissociation instead of the hydrolytic step in its activation mechanism. Muscle myosin and kinesin have two head domains.

Even twelve years later, what continued to remain misunderstood were the varying degrees of thin filament activation between pre- or post-power stroke myosin. Myosin’s kinetic properties had remained vague, and many techniques had been employed to further investigate what was left unknown. One of these techniques actually was instigated by Taylor and B. Finlayson in 1969 through the proton release. In 1987, S. Rosenfeld and Taylor evaluated the regulatory mechanism of actin-sub fragment 1 nucleoside triphosphate. They were interested in the influence that calcium binding to regulated actin has on ATPase cycle rates. For the hydrolysis step, there was only a small change in the presence of calcium. On the other hand, for the dissociation of the ligand and products, the presence of calcium for ATP led to an increased rate by 10-20-fold. These results showed Rosenfeld and Taylor that the particular steps in the ATPase cycle that were most impacted by the presence of calcium were the transition steps, followed by the dissociation of the ligand from the active site.

The actomyosin ATP hydrolysis cycle in muscle motility was intended to show a direct correlation in the regulation of ATP hydrolysis and the power stroke. However, experiments that exhibited an absence of ATP hydrolysis could not explain regulation. 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. In their research, they confirm that the thin filament activity is primarily influenced by the rate of inorganic phosphate dissociation. In addition, they observed that the regulatory focal point of the thin filament, or the step that releases the inorganic phosphate, is dependent upon myosin’s conformation, as well as the bonded state of the thin filament. On May 1, 2001, Taylor was elected Member of the National Academy of Sciences. He was elected for his crucial contributions to the biochemistry of muscle contraction. Taylor is recognized as the "father of cytoskeletal research".