A two-state kinetic model predicts that kinesin's randomness parameter has a non-monotonic ATP dependence if ATP binds with both heads attached, but a monotonic decrease if the trailing head detaches first.
(2015) Kinetics of nucleotide-dependent structural transitions in the kinesin-1 hydrolysis cycle.Proceedings of the National Academy of Sciences112(52):E7186– E7193
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How kinesin waits for ATP affects the nucleotide and load dependence of the stepping kinetics
A two-state kinetic model predicts that kinesin's randomness parameter has a non-monotonic ATP dependence if ATP binds with both heads attached, but a monotonic decrease if the trailing head detaches first.