Abstract
Single-molecule Förster Resonance Energy Transfer (smFRET) is a useful technique to probe conformational changes within bio-macromolecules. Here, we introduce how to perform smFRET measurements in solution to investigate RNA remodeling and RNA–protein interactions. In particular, we focus on how the close-to-open transition of an antiterminator hairpin is influenced by the binding of the antitermination protein and the competition by oligonucleotides.
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Acknowledgments
This work was supported by the Agence Nationale de la Recherche (ANR 2010 BLAN 1525 01 to E.M.), a “Chercheur d’Avenir” grant from the Region Languedoc Roussillon to E.M., the GIS “IBiSA: Infrastructures en Biologie Sante et Agronomie” and a postdoctoral grant from the Université Montpellier I to S.A.-B.
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Ait-Bara, S., Clerté, C., Margeat, E. (2015). Single-Molecule FRET Characterization of RNA Remodeling Induced by an Antitermination Protein. In: Boudvillain, M. (eds) RNA Remodeling Proteins. Methods in Molecular Biology, vol 1259. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2214-7_21
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DOI: https://doi.org/10.1007/978-1-4939-2214-7_21
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