(A) Schematics of the kinesin team. In the depicted case, the team consists of three kinesins and two of them are shown as bound to the microtubule and move at the velocities and , respectively. Since the elastic linkage between the dimers stretches generating the forces and . (B) Representation of the force–velocity relation used in the model. (C) Representation of the dependence of the unbinding rate on the applied force. (D) Example of a simulation for a complex size with three dimers. The blue graph is the position of the center of mass of the complex as a function of time (left axis), red graph shows the number of dimers attached to the microtubule at each time point. (right axis). (E–F) Velocity, run length and their standard deviations as a function of the complex size for different values of . Other parameters of the simulation are: V = 50 nm/s, = 20 nm/s; = 1 pN; = 0.55 s−1; = 0.08 s−1; = 4 s−1. (G) Comparison between experimental data (blue) and best fit (see values of objective function in Table 5) of the simplified theoretical model without force dependence (red). (H–I) Velocity, run length and their standard deviations as a function of the complex size for best parameters of the complete model. Data are shown for red— = 0.2 pN; = 0.57 s−1; = 3.7 s−1; magenta—= 1 pN; = 0.55 s−1; = 4 s−1; green— = 4 pN; = 0.49 s−1; = 5.3 s−1; Other parameters for all simulations: V = 50 nm/s, = 20 nm/s; = 0.08 s−1; = 0.03 pN/nm.