ArticleCold Spring Harbor protocols2012
Fluorescent labeling of myosin V for polarized total internal reflection fluorescence microscopy (polTIRFM) motility assays.
Article in Cold Spring Harbor protocols, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- Elongation factor G initiates translocation through a power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The polarized total internal reflection fluorescence microscopy (polTIRFM) processive motility assay for myosin V.Cold Spring Harbor protocols · 2012Article
- Fluorescent labeling of calmodulin with bifunctional rhodamine.Cold Spring Harbor protocols · 2012Article
- Orientation and rotational motions of single molecules by polarized total internal reflection fluorescence microscopy (polTIRFM).Cold Spring Harbor protocols · 2012Article
- Preparation of filamentous actin for polarized total internal reflection fluorescence microscopy (polTIRFM) motility assays.Cold Spring Harbor protocols · 2012Article
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Authors and funding
5 authors.
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Abstract
Polarized total internal reflection fluorescence microscopy (polTIRFM) can be used to detect the spatial orientation and rotational dynamics of single molecules. polTIRFM determines the three-dimensional angular orientation and the extent of wobble of a fluorescent probe bound to the macromolecule of interest. This protocol describes how to exchange bifunctional rhodamine-calmodulin (BR-CaM) for wild-type calmodulin (WT-CaM) on the lever arm of myosin V. BR-CaM is exchanged at low stoichiometry (∼0.4 BR-CaM per double-headed myosin V) to obtain myosin V molecules with one BR-CaM and to limit the proportion of myosin V molecules with two or more probes. The stoichiometry is very sensitive to the concentration of calcium during the exchange reaction. The labeled myosin V can subsequently be used for investigating the motility of myosin V in vitro with a polTIRFM processive motility assay, which is performed on substrate-attached actin.
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