Kinetics of ADP dissociation from the trail and lead heads of actomyosin V following the power stroke.

@article{Forgacs2008KineticsOA,
  title={Kinetics of ADP dissociation from the trail and lead heads of actomyosin V following the power stroke.},
  author={Eva Forgacs and Suzanne Cartwright and Takeshi Sakamoto and James R Sellers and John E. T. Corrie and Martin R Webb and Howard D. White},
  journal={The Journal of biological chemistry},
  year={2008},
  volume={283 2},
  pages={766-73}
}
Myosin V is a cellular motor protein, which transports cargos along actin filaments. It moves processively by 36-nm steps that require at least one of the two heads to be tightly bound to actin throughout the catalytic cycle. To elucidate the kinetic mechanism of processivity, we measured the rate of product release from the double-headed myosin V-HMM using a new ATP analogue, 3'-(7-diethylaminocoumarin-3-carbonylamino)-3'-deoxy-ATP (deac-aminoATP), which undergoes a 20-fold increase in… CONTINUE READING
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