Sedimentation studies on the kinesin motor domain constructs K401, K366, and K341.

@article{Correia1995SedimentationSO,
  title={Sedimentation studies on the kinesin motor domain constructs K401, K366, and K341.},
  author={John J. Correia and Susan P Gilbert and Michelle L. Moyer and Kenneth A Johnson},
  journal={Biochemistry},
  year={1995},
  volume={34 14},
  pages={
          4898-907
        }
}
Bacterial expressed kinesin motor domains hydrolyze ATP and promote microtubule-dependent motility. It has routinely been assumed that motor domain preparations are monomeric on the basis of the presumption that dimerization is mediated by the stalk region. However, experimental verification of the oligomeric state of the kinesin construct is required to interpret the results from single-molecule motility assays as well as presteady-state kinetic experiments. We have measured directly the state… CONTINUE READING
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