Dynamics of kinesin motor proteins under longitudinal and sideways loads

The available single-molecule data showed that different species of N-terminal kinesin molecular motors have very different features on dependences of run length and dissociation rate upon longitudinal load acting on stalks of the motors. The prior single-molecule data for Loligo pealei kinesin-1 indicated that the sideways load has only a weak effect on the velocity, but even a small sideways load can cause a large reduction in the run length. However, these puzzling experimental data remain to be explained and the underlying physical mechanisms are unclear. Here, based on our proposed model we study analytically the dynamics of the N-terminal kinesin motors such as Loligo pealei kinesin-1, Drosophila kinesin-1, truncated kinesin-5/Eg5, truncated kinesin-12/Kif15, kinesin-2/Kif17 and kinesin-2/Kif3AB dimers under both longitudinal and sideways loads. The theoretical results explain quantitatively the available experimental data and provide predictions. The physical mechanism of different kinesin species showing very different features on the load-dependent dynamics and the physical mechanism of the effect of the sideways load on the dynamics are revealed.