Article
Rapid double 8-nm steps by a kinesin mutant.
The EMBO journal - 4 Aug 2004
Higuchi Hideo, Bronner Christian Eric, Park Hee-Won, Endow Sharyn A
Abstract excerpt
The mechanism by which conventional kinesin walks along microtubules is poorly understood, but may involve alternate binding to the microtubule and hydrolysis of ATP by the two heads. Here we report a single amino-acid change that affects stepping by the motor. Under low force or low ATP concentration, the motor moves by successive 8-nm steps in single-motor laser-trap assays, indicating that the mutation does...
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