Alternating-Site Mechanism of Kinesin-1 Characterized by Single-Molecule FRET Using Fluorescent ATP Analogues

Kinesin-1 motor proteins move along microtubules in repetitive steps of 8 nm at the expense of ATP. To determine nucleotide dwell times during these processive runs, we used a Förster resonance energy transfer method at the single-molecule level that detects nucleotide binding to kinesin motor heads...

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Detalhes bibliográficos
Main Authors: Verbrugge, Sander, Lechner, Bettina, Woehlke, Günther, Peterman, Erwin J.G.
Formato: Artigo
Idioma:Inglês
Publicado em: The Biophysical Society 2009
Assuntos:
Muscle, Molecular Motors, and Cell Motility
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2711353/
https://ncbi.nlm.nih.gov/pubmed/19580755
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpj.2009.02.073
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