Measuring complexation by single-molecule fluorescence anisotropy
Analyst, ISSN: 0003-2654, Vol: 133, Issue: 7, Page: 870-873
2008
- 10Citations
- 15Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Article Description
The complexation of a fluorescent probe by a target protein was observed by single-molecule fluorescence anisotropy. Free and bound states, heterogeneities, and rare binding events can all be observed by this approach. Fluorophore-conjugated biotin was used to bind to NeutrAvidin as a proof-of-concept case. Molecular interactions were observed that could not be elucidated with conventional (ensemble) measurements. © The Royal Society of Chemistry.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=48249102338&origin=inward; http://dx.doi.org/10.1039/b800110c; http://www.ncbi.nlm.nih.gov/pubmed/18575637; https://xlink.rsc.org/?DOI=b800110c; https://dx.doi.org/10.1039/b800110c; https://pubs.rsc.org/en/content/articlelanding/2008/an/b800110c
Royal Society of Chemistry (RSC)
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