ArticleProtein science : a publication of the Protein Society2023
FRETing about the details: Case studies in the use of a genetically encoded fluorescent amino acid for distance-dependent energy transfer.
Article in Protein science : a publication of the Protein Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Genetic Code Expansion for Site-Specific Encoding of a Switchable, Intrinsic Fluorophore-Quencher Pair to Monitor Protein Dynamics.bioRxiv : the preprint server for biology · 2026Article
- Three-color single-molecule fluorescence resonance energy transfer to study macromolecular dynamics.Current opinion in structural biology · 2026Review
- Interactions of Neurodegenerative Disease Positron Emission Tomography Imaging Probe Candidates with the C-Terminus of α-Synuclein Fibrils.Chembiochem : a European journal of chemical biology · 2025Article
- Expanding the fluorescence toolkit: molecular design, synthesis and biological application of unnatural amino acids.Chemical science · 2025Review
- Improved Large-Scale Synthesis of Acridonylalanine for Diverse Peptide and Protein Applications.Bioconjugate chemistry · 2024Article
- Long-distance tmFRET using bipyridyl- and phenanthroline-based ligands.Biophysical journal · 2024Article
- Long-distance tmFRET using bipyridyl- and phenanthroline-based ligands.bioRxiv : the preprint server for biology · 2024Article
- FRETing about the details: Case studies in the use of a genetically encoded fluorescent amino acid for distance-dependent energy transfer.Protein science : a publication of the Protein Society · 2023Article
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14 authors.
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Abstract
Förster resonance energy transfer (FRET) is a valuable method for monitoring protein conformation and biomolecular interactions. Intrinsically fluorescent amino acids that can be genetically encoded, such as acridonylalanine (Acd), are particularly useful for FRET studies. However, quantitative interpretation of FRET data to derive distance information requires careful use of controls and consideration of photophysical effects. Here we present two case studies illustrating how Acd can be used in FRET experiments to study small molecule induced conformational changes and multicomponent biomolecular complexes.
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