ArticleBiophysical journal2007
Fluorescence depolarization studies of filamentous actin analyzed with a genetic algorithm.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Who cites it
2 citing papers in PubMed, 18 citations in OpenAlex.
- In vivo imaging of the actin polymerization state with two-photon fluorescence anisotropy.Biophysical journal · 2012Article
- The crystal structure of the C-terminus of adseverin reveals the actin-binding interface.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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Authors and funding
5 authors at 3 institutions in 1 country.
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Abstract
A new method, in which a genetic algorithm was combined with Brownian dynamics and Monte Carlo simulations, was developed to analyze fluorescence depolarization data collected by the time-correlated single photon-counting technique. It was applied to studies of BODIPY-labeled filamentous actin (F-actin). The technique registered the local order and reorienting motions of the fluorophores, which were covalently coupled to cysteine 374 (C374) in actin and interacted by electronic energy migration within the actin polymers. Analyses of F-actin samples composed of different fractions of labeled actin molecules revealed the known helical organization of F-actin, demonstrating the usefulness of this technique for structure determination of complex protein polymers. The distance from the filament axis to the fluorophore was found to be considerably less than expected from the proposed position of C374 at a high filament radius. In addition, polymerization experiments with BODIPY-actin suggest a 25-fold more efficient signal for filament formation than pyrene-actin.
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