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Rapid double 8-nm steps by a kinesin mutant
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 concentrati...
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| Pubblicato in: | EMBO J |
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| Autori principali: | , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Nature Publishing Group
2004
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC514923/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/15257294/ https://ncbi.nlm.nih.govhttps://doi.org/10.1038/sj.emboj.7600306 |
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