Measuring complexation by single-molecule fluorescence anisotropy
Literature Information
Publication Date
2008-04-02
DOI
10.1039/B800110C
Impact Factor
4.616
Authors
Sean M. Burrows, Dimitri Pappas
View Original
Abstract
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.
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Analyst publishes analytical and bioanalytical research that reports premier fundamental discoveries and inventions, and the applications of those discoveries, unconfined by traditional discipline barriers.
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