Mechanical control of the directional stepping dynamics of the kinesin motor.

ABSTRACT: Among the multiple steps constituting the kinesin mechanochemical cycle, one of the most interesting events is observed when kinesins move an 8-nm step from one microtubule (MT)-binding site to another. The stepping motion that occurs within a relatively short time scale ( approximately 100 mus) is, however, beyond the resolution of current experiments. Therefore, a basic understanding to the real-time dynamics within the 8-nm step is still lacking. For instance, the rate of power stroke (or conformational change) that leads to the undocked-to-docked transition of neck-linker is not known, and the existence of a substep during the 8-nm step still remains a controversial issue in the kinesin community. By using explicit structures of the kinesin dimer and the MT consisting of 13 protofilame

SUBMITTER: Hyeon C 

PROVIDER: S-EPMC2077265 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature