ReviewJournal of fluorescence2004
Utility and considerations of donor-donor energy migration as a fluorescence method for exploring protein structure-function.
Review in Journal of fluorescence, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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
7 citing papers in PubMed.
- Conformational Dynamic Studies of Prokaryotic Potassium Channels Explored by Homo-FRET Methodologies.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Designed fluorescent probes reveal interactions between amyloid-beta(1-40) peptides and GM1 gangliosides in micelles and lipid vesicles.Biophysical journal · 2010Article
- Fluorescence spectroscopic properties analysed within the extended Förster theory with application to biomacromolecular systems.Journal of fluorescence · 2009Article
- Fluorescence depolarization studies of filamentous actin analyzed with a genetic algorithm.Biophysical journal · 2007Article
- Conformational motion of the ABC transporter MsbA induced by ATP hydrolysis.PLoS biology · 2007Article
- Distance measurements by fluorescence energy homotransfer: evaluation in T4 lysozyme and correlation with dipolar coupling between spin labels.Biophysical journal · 2007Article
- Energy migration alters the fluorescence lifetime of Cerulean: implications for fluorescence lifetime imaging Forster resonance energy transfer measurements.Journal of biomedical opticsArticle
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This review aims at surveying the use of electronic energy transport between chemically identical fluorophores (i.e. donors) in studies of various protein systems. Applications of intra- and interprotein energy migration are presented that make use of polarised steady-state and time-resolved fluorescence spectroscopic techniques. The donor-donor energy migration (DDEM) and the partial donor-donor energy migration (PDDEM) models for calculating distances between donor groups are exposed together with the most recent development of an extended Forster theory (EFT). Synthetic fluorescence depolarisation data that mimic time-correlated single photon counting experiments were generated using the EFT, and then further re-analysed by the different models. The results obtained were compared with the known parameters used to generate EFT data. Aspects on how to adopt the EFT in the analyses of time-correlated single photon counting experiments are also presented, as well as future aspects on using energy migration for examining protein structure.
Indexed as
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Registered trials
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