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- W2024754281 abstract "The effects of timescale and force transducer stiffness on kinesin detachment from the microtubule surface, as represented by the alpha-beta tubulin dimer, have been investigated using Steered Molecular Dynamics (SMD) simulations. By decreasing the pulling speed and using a softer spring in the SMD simulation, a kinesin detachment force in the range of 100 to 150 pN is obtained. This result is in better agreement than previous SMD calculations with experimental measurements of the detachment force obtained using optical traps and atomic force microscopy.Moreover, the differences between the simulated and experimentally measured kinesin detachment forces may be attributed to the experimental configuration a microbead attached to an 80 nanometer coiled-coil stalk. The stalk acts as a long moment arm on the neck liner of kinesin, thus causing underestimation of the actual detachment force at the kinesin-microtubule interface by a factor of 5 to 7. Taking into account the effect of the moment arm, the experimental results suggest an actual stall force for kinesin-microtubule binding in the range of 60 to 150 pN. This range of forces brackets the detachment force calculated in the SMD simulations.It was also noted that different mechanisms of kinesin detachment from the tubulin dimer are observed for different selected values of the SMD pulling parameters. Specifically, at low pulling speed and for a soft spring stiffness, the detachment process reveals conformational changes that involve the translocation and rotation of the kinesin head as well as the switch II region. Switch II has been identified as the main binding region between kinesin and the microtubule surface." @default.
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- W2024754281 date "2011-02-01" @default.
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- W2024754281 title "Steered Molecular Dynamics Simulation of Kinesin Detachment from the Microtubule Surface" @default.
- W2024754281 doi "https://doi.org/10.1016/j.bpj.2010.12.1278" @default.
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