Ontology highlight
ABSTRACT:
SUBMITTER: Verbrugge S
PROVIDER: S-EPMC2764935 | biostudies-literature | 2009 Oct
REPOSITORIES: biostudies-literature
Verbrugge Sander S Lansky Zdenek Z Peterman Erwin J G EJ
Proceedings of the National Academy of Sciences of the United States of America 20091001 42
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 timesc ...[more]