Literature DB >> 25579596

Single-molecule FRET characterization of RNA remodeling induced by an antitermination protein.

Soraya Ait-Bara1, Caroline Clerté, Emmanuel Margeat.   

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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Year:  2015        PMID: 25579596     DOI: 10.1007/978-1-4939-2214-7_21

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  2 in total

Review 1.  Life under the Microscope: Single-Molecule Fluorescence Highlights the RNA World.

Authors:  Sujay Ray; Julia R Widom; Nils G Walter
Journal:  Chem Rev       Date:  2018-01-24       Impact factor: 60.622

2.  Competitive folding of RNA structures at a termination-antitermination site.

Authors:  Soraya Ait-Bara; Caroline Clerté; Nathalie Declerck; Emmanuel Margeat
Journal:  RNA       Date:  2017-02-24       Impact factor: 4.942

  2 in total

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