ArticleCold Spring Harbor protocols2012
The polarized total internal reflection fluorescence microscopy (polTIRFM) processive motility assay for myosin V.
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 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- The polarized total internal reflection fluorescence microscopy (polTIRFM) twirling filament assay.Cold Spring Harbor protocols · 2012Article
- The acquisition and analysis of polarized total internal reflection fluorescence microscopy (polTIRFM) data.Cold Spring Harbor protocols · 2012Article
- Construction of flow chambers 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 the processive motility assay for investigating the motility of myosin V in vitro. Biotin-Alexa actin filaments are fixed to a slide by biotin/streptavidin linkages and aligned with the microscope x-axis by fluid flow. The orientation of a rhodamine-calmodulin (CaM) probe bound to a single myosin V molecule is determined as it moves along an actin filament. Excess wild-type calmodulin (WT-CaM) is present in the buffer solution to replenish lost CaM from the myosin lever arm. The techniques for myosin V should be generally applicable to other single-molecule experiments where angular changes have an important mechanistic role in their biological function.
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