2002 Volume 42 Issue 4 Pages 156-161
Kinesin motors are mechano-enzymes that hydrolyze ATP to generate force and directional movement along a microtubule. Nucleotide-dependent conformational changes of the head and neck region of kinesin have been shown by cryoelectron microscopy and spectroscopic techniques. Single molecule analysis supports key predictions of the hand-over-hand model for motility of dimeric conventional kinesin, whereas the discovery of a processive one-headed kinesin strongly supports the biased Brownian ratchet model. In this short review, we summarize the present status of research on the mechanism of kinesin motility.
