ArticleCold Spring Harbor protocols2012
The polarized total internal reflection fluorescence microscopy (polTIRFM) twirling filament assay.
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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Who cites it
3 citing papers in PubMed, 4 citations in OpenAlex.
- The acquisition and analysis of polarized total internal reflection fluorescence microscopy (polTIRFM) data.Cold Spring Harbor protocols · 2012Article
- The polarized total internal reflection fluorescence microscopy (polTIRFM) processive motility assay for myosin V.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 twirling filament assay, so named because actin sometimes twirls about its own axis as it is translocated by myosin. A gliding filament assay is constructed in which a sparsely labeled actin filament (0.3% of the actin monomers contain 6'- iodoacetamidotetramethylrhodamine [IATR]) is translocated by a field of unlabeled myosin V fixed to the surface. The polTIRFM twirling assay differs from a standard gliding filament assay in that full filaments are not visible, but rather individual fluorophores are spaced along each filament. The goal is to investigate possible rotational motions of the actin filament about its axis (i.e., twirling) by measuring the spatial angle of the fluorescent probe as a function of time. Successful assays contain microscopic fields of approximately 50 isolated points of fluorescence that move across the field in the presence of ATP. Actin is usually translocated by more than one myosin molecule, depending on the filament length and the myosin surface density. Sparsely labeled filaments are required because the orientation of only one probe can be resolved at a time.
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Registered trials
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