Thormählen M, Marx A, Müller S A, Song Y, Mandelkow E M, Aebi U, Mandelkow E
Max-Planck-Unit for Structural Molecular Biology, Notkestrasse 85, Hamburg, D-22603, Germany.
J Mol Biol. 1998 Feb 6;275(5):795-809. doi: 10.1006/jmbi.1997.1503.
The binding stoichiometry of kinesin to microtubules was determined using several biochemical and biophysical approaches (chemical crosslinking, binding assays, scanning transmission electron microscopy (STEM), image reconstruction, and X-ray scattering). The results show that each tubulin dimer associates with one kinesin head, irrespective of whether kinesin occurs in a monomeric or dimeric form in solution. Moreover, these heads appear to align along the protofilament axis generating a 16 nm periodicity of successive kinesin dimers. This is consistent with a "tightrope" model of movement where the first head of the dimer provides a guiding signal for the following one.
使用多种生化和生物物理方法（化学交联、结合测定、扫描透射电子显微镜（STEM）、图像重建和X射线散射）确定了驱动蛋白与微管的结合化学计量。结果表明，每个微管蛋白二聚体与一个驱动蛋白头部结合，无论驱动蛋白在溶液中是以单体还是二聚体形式存在。此外，这些头部似乎沿着原纤维轴排列，产生连续驱动蛋白二聚体的16纳米周期性。这与“走钢丝”运动模型一致，即二聚体的第一个头部为后续头部提供引导信号。
