G-quadruplex structure and stability illuminated by 2-aminopurine phasor plots. Buscaglia, R., Jameson, D. M, & Chaires, J. B Nucleic acids research, 40(9):4203–15, May, 2012. ![G-quadruplex structure and stability illuminated by 2-aminopurine phasor plots. [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex The use of time-resolved fluorescence measurements in studies of telomeric G-quadruplex folding and stability has been hampered by the complexity of fluorescence lifetime distributions in solution. The application of phasor diagrams to the analysis of time-resolved fluorescence measurements, collected from either frequency-domain or time-domain instrumentation, allows for rapid characterization of complex lifetime distributions. Phasor diagrams are model-free graphical representations of transformed time-resolved fluorescence results. Simplification of complex fluorescent decays by phasor diagrams is demonstrated here using a 2-aminopurine substituted telomeric G-quadruplex sequence. The application of phasor diagrams to complex systems is discussed with comparisons to traditional non-linear regression model fitting. Phasor diagrams allow for the folding and stability of the telomeric G-quadruplex to be monitored in the presence of either sodium or potassium. Fluorescence lifetime measurements revealed multiple transitions upon folding of the telomeric G-quadruplex through the addition of potassium. Enzymatic digestion of the telomeric G-quadruplex structure, fluorescence quenching and Förster resonance energy transfer were also monitored through phasor diagrams. This work demonstrates the sensitivity of time-resolved methods for monitoring changes to the telomeric G-quadruplex and outlines the phasor diagram approach for analysis of complex time-resolved results that can be extended to other G-quadruplex and nucleic acid systems.
@article{Buscaglia2012,
title = {G-quadruplex structure and stability illuminated by 2-aminopurine phasor plots.},
volume = {40},
issn = {1362-4962},
url = {http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3351194&tool=pmcentrez&rendertype=abstract},
doi = {10.1093/nar/gkr1286},
abstract = {The use of time-resolved fluorescence measurements in studies of telomeric G-quadruplex folding and stability has been hampered by the complexity of fluorescence lifetime distributions in solution. The application of phasor diagrams to the analysis of time-resolved fluorescence measurements, collected from either frequency-domain or time-domain instrumentation, allows for rapid characterization of complex lifetime distributions. Phasor diagrams are model-free graphical representations of transformed time-resolved fluorescence results. Simplification of complex fluorescent decays by phasor diagrams is demonstrated here using a 2-aminopurine substituted telomeric G-quadruplex sequence. The application of phasor diagrams to complex systems is discussed with comparisons to traditional non-linear regression model fitting. Phasor diagrams allow for the folding and stability of the telomeric G-quadruplex to be monitored in the presence of either sodium or potassium. Fluorescence lifetime measurements revealed multiple transitions upon folding of the telomeric G-quadruplex through the addition of potassium. Enzymatic digestion of the telomeric G-quadruplex structure, fluorescence quenching and Förster resonance energy transfer were also monitored through phasor diagrams. This work demonstrates the sensitivity of time-resolved methods for monitoring changes to the telomeric G-quadruplex and outlines the phasor diagram approach for analysis of complex time-resolved results that can be extended to other G-quadruplex and nucleic acid systems.},
number = {9},
journal = {Nucleic acids research},
author = {Buscaglia, Robert and Jameson, David M and Chaires, Jonathan B},
month = may,
year = {2012},
pmid = {22241767},
keywords = {\#nosource, 2-Aminopurine, 2-Aminopurine: chemistry, DNA, DNA: chemistry, Fluorescence Resonance Energy Transfer, G-Quadruplexes, Plant Proteins, Plant Proteins: metabolism, Single-Strand Specific DNA and RNA Endonucleases, Single-Strand Specific DNA and RNA Endonucleases:, Telomere, Telomere: chemistry},
pages = {4203--15},
}
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