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Measuring protein structural dynamics |
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Single molecule FRET allows the measurement of distances and distance changes between two fluorescent molecules in a biomolecular complexes, down to the Angstrom and the microsecond timescales. smFRET measurement can be performed in vitro:
All projects are run as collaborations. Please This email address is being protected from spambots. You need JavaScript enabled to view it. for help choosing the most appropriate approach. We also provide advice to design your experiment and support with fluorescent labeling and data analysis. After a meeting, we can run a few experiments to assess the feasibility of the approach. Then a collaboration scheme is defined between the team and the facility. Our R&D division can also implement specific adaptations for your project if needed. |
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Measurements of distances changes within E. Coli and MTB transcription complexes using single molecule FRET (from Vishwakarma et al.) |
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Selected publications: Quast R.B., Fatemi F., Kranendonk M., Margeat E.*, Truan G.* Accurate Determination of CPR Conformational Equilibrium by smFRET using Dual Orthogonal Non-Canonical Amino Acid Labeling, ChemBioChem, 2019, 20(5):659-666 Vishwakarma RK, Cao AM, Morichaud Z, Perumal AS, Margeat E, Brodolin K, Single-molecule analysis reveals the mechanism of transcription activation in M. Tuberculosis. Sci Adv, 2018 Ait-Bara S, Clerte C, Declerck N, Margeat E. Competitive folding of RNA structures at a termination / antitermination site. RNA, 2017 Ait-Bara S, Clerte C, Margeat E. Single-Molecule FRET Characterization of RNA Remodeling Induced by an Antitermination Protein, Methods Mol Biol, 2015 Olofsson L, Felekyan S, Doumazane E, Scholler P, Fabre L, Zwier JM, Rondard P, Seidel CA, Pin JP, Margeat E. Fine tuning of sub-millisecond conformational dynamics controls metabotropic glutamate receptors agonist efficacy, Nat Commun, 2014
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SmFRET TCSPC
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TIRF / 3D MFM
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