Kinesin's step dissected with single-motor FRET.

@article{Verbrugge2009KinesinsSD,
  title={Kinesin's step dissected with single-motor FRET.},
  author={Sander A. J. Verbrugge and Zdenek Lansky and Erwin J G Peterman},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 42},
  pages={17741-6}
}
The motor protein Kinesin-1 drives intracellular transport along microtubules, with each of its two motor domains taking 16-nm steps in a hand-over-hand fashion. The way in which a single-motor domain moves during a step is unknown. Here, we use Förster resonance energy transfer (FRET) between fluorescent labels on both motor domains of a single kinesin. This approach allows us to resolve the relative distance between the motor domains and their relative orientation, on the submillisecond… CONTINUE READING