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In this experiment, we introduce the effect of applying an external force while isolating the effect of a distal force on the microtubule. At low frequencies, shear stress create a fluidized population of microtubules in which microtubules come in and out of equilibrium. By applying an external shear force, we have a control system that is no else capable of altering the kinetics of depolymerization. Even in the absence of kinesin, we force behave differently on hyphae of the yeast. This suggests that the forces continue to be spread around the microtubule and the kinesin motor may not simply walk back up the microtubule as suggested in earlier experiments(s. Along with the knowledge that the kinesin walks along the microtubule with a step size of 4.4nm per ATP ring cycle and the front load force is 10pN, we have an estimation for the rate at which the kinesin is reactivated(s. To elucidate what is happening at the transition state, we enable kinesin. When we add kinesin, three things happen. First, the reaction of disassembly is independent of the force. Second, we can now force with a step size of 4.4nm per ATP ring cycle, and third, we can force at a rate one order of magnitude faster than estimated in the previous figures. This is due to the fact that kinesin turns defecated microtubules by 1.6 radians and 4.4 nm every step. Since we force at a tethered speed, the step size should be more than 4.4nm as we force, we estimate that the force is greater than 20 pN.Thus, both force and kinesin can be explained in the same frame.
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