ArticleCold Spring Harbor protocols2012
Fluorescent labeling of calmodulin with bifunctional rhodamine.
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, 9 citations in OpenAlex.
- Article
- Elongation factor G initiates translocation through a power stroke.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Orientation and rotational motions of single molecules by polarized total internal reflection fluorescence microscopy (polTIRFM).Cold Spring Harbor protocols · 2012Article
- Fluorescent labeling of myosin V for polarized total internal reflection fluorescence microscopy (polTIRFM) motility assays.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.
Funding
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 label chicken calmodulin (CaM) with bifunctional rhodamine (BR) at two engineered cysteine (Cys) residues (P66C and A73C) so that it cross-links the two Cys sites. The resulting BR-CaM protein is then purified by high-performance liquid chromatography (HPLC) and concentrated by filter centrifugation. To confirm that the two Cys residues in the labeled CaM are actually cross-linked by BR, a sample of purified BR-CaM is digested by an endoproteinase and analyzed by mass spectrometry. The BR-CaM can then be used to label myosin V, which can in turn be used in a polTIRFM processive motility assay.
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