ArticleBiophysical journal2024
Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET.
Article in Biophysical journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Article
- A PIP2-stabilized syntaxin-1a structure mapped with transition metal ion FRET and unnatural fluorescent amino acids at the plasma membrane.Structure (London, England : 1993) · 2026Article
- Interrogating the structure and function of the human voltage-gated proton channel (hHbioRxiv : the preprint server for biology · 2025Article
- 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
- Structural insights into GTP-coupled conformational changes in Mfn1 revealed by time-resolved transition metal ion FRET.bioRxiv : the preprint server for biology · 2025Article
- Advances in FRET methodologies for probing molecular interactions.Biophysical journal · 2025Article
- Domain coupling in allosteric regulation of SthK measured using time-resolved transition metal ion FRET.eLife · 2025Article
- Improved Large-Scale Synthesis of Acridonylalanine for Diverse Peptide and Protein Applications.Bioconjugate chemistry · 2024Article
- Article
- Ligand-Coupled Conformational Changes in a Cyclic Nucleotide-Gated Ion Channel Revealed by Time-Resolved Transition Metal Ion FRET.bioRxiv : the preprint server for biology · 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
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8 authors at 2 institutions in 1 country.
Funding
Abstract
Proteins are the workhorses of biology, orchestrating a myriad of cellular functions through intricate conformational changes. Protein allostery, the phenomenon where binding of ligands or environmental changes induce conformational rearrangements in the protein, is fundamental to these processes. We have previously shown that transition metal Förster resonance energy transfer (tmFRET) can be used to interrogate the conformational rearrangements associated with protein allostery and have recently introduced novel FRET acceptors utilizing metal-bipyridyl derivatives to measure long (>20 Å) intramolecular distances in proteins. Here, we combine our tmFRET system with fluorescence lifetime measurements to measure the distances, conformational heterogeneity, and energetics of maltose-binding protein, a model allosteric protein. Time-resolved tmFRET captures near-instantaneous snapshots of distance distributions, offering insights into protein dynamics. We show that time-resolved tmFRET can accurately determine distance distributions and conformational heterogeneity of proteins. Our results demonstrate the sensitivity of time-resolved tmFRET in detecting subtle conformational or energetic changes in protein conformations, which are crucial for understanding allostery. In addition, we extend the use of metal-bipyridyl compounds, showing that Cu(phen)
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