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Fig. 8. Model to investigate how detyrosination affects kinesin-1 behaviour on MTs. (A) Basis for the model. Circles represent binding sites along MTs, n=0 corresponds to the minus-end of the MT, and n=N is the plus-end. Kinesin-1 can bind to an MT with an on-rate of k_on, detach with an off-rate of k_off, and can either move towards the plus-end (taking unit steps) at a rate of k₊ or towards the minus-end at a rate of k_–. For details of the model see Materials and Methods. (B) Results obtained when using the model. Stationary number density distribution of kinesin-1 was obtained using equations 10, 11, 12; average number density, average flux and average velocity as a function of tyrosinated tubulin, were obtained using equations 13, 14, 15.

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