Edwin W Taylor

We study the mechanism of molecular motors, myosin with actin and kinesin with microtubules. The objective is to show how the steps in the kinetic mechanism determine the structural changes which produce force and motion. To disect the steps in the system mutant kinesins, expressed in bacteria, are studied in which a step in the mechanism is blocked. The results are correlated with the structure of the protein and its motility properties determined by in vitro assay.

We study the mechanism of molecular motors, myosin with actin and kinesin with microtubules. The objective is to show how the steps in the kinetic mechanism determine the structural changes which produce force and motion. To disect the steps in the system mutant kinesins, expressed in bacteria, are studied in which a step in the mechanism is blocked. The results are correlated with the structure of the protein and its motility properties determined by in vitro assay.

Ma, Y. Z. and Taylor, E. W. (1997). "Interacting head mechanism of microtubule-kinesin ATPase." J Biol Chem 272: 724-30.   PubMed Citation

Ma, Y. Z. and Taylor, E. W. (1997). "Kinetic mechanism of a monomeric kinesin construct." J Biol Chem 272: 717-23.   PubMed Citation

Pechatnikova, E. and Taylor, E. W. (1997). "Kinetic mechanism of monomeric non-claret disjunctional protein (Ncd) ATPase." J Biol Chem 272: 30735-40.   PubMed Citation

Ma, Y. Z. and Taylor, E. W. (1997). "Interacting head mechanism of microtubule-kinesin ATPase." J Biol Chem 272: 724-30.   PubMed Citation

Ma, Y. Z. and Taylor, E. W. (1997). "Kinetic mechanism of a monomeric kinesin construct." J Biol Chem 272: 717-23.   PubMed Citation

Pechatnikova, E. and Taylor, E. W. (1997). "Kinetic mechanism of monomeric non-claret disjunctional protein (Ncd) ATPase." J Biol Chem 272: 30735-40.   PubMed Citation