Abstract
The detection of dynamic conformational changes in proteins in live cells is challenging. Live-cell FRET (Förster Resonance Energy Transfer) is an example of a noninvasive technique that can be used to achieve this goal at nanometer resolution. FRET-based assays are dependent on the presence of fluorescent probes, such as CFP- and YFP-conjugated protein pairs. Here, we describe an experimental protocol in which live-cell FRET was used to measure conformational changes in caveolin-1 (Cav-1) oligomers on the surface of plasmalemma vesicles, or caveolae.
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Zimnicka, A.M., Chen, Z., Toth, P.T., Minshall, R.D. (2020). Live-Cell FRET Imaging of Phosphorylation-Dependent Caveolin-1 Switch. In: Blouin, C. (eds) Caveolae. Methods in Molecular Biology, vol 2169. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0732-9_7
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DOI: https://doi.org/10.1007/978-1-0716-0732-9_7
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