ArticleNature chemistry2020
Directional conformer exchange in dihydrofolate reductase revealed by single-molecule nanopore recordings.
Article in Nature chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 123 citations in OpenAlex.
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- Engineering a Monomeric Nanopore Scaffold for Multiplexed Protein Detection.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Enzyme-assisted nanopore sensor for sensitive and multiplexed detection of microRNAs.Journal of nanobiotechnology · 2025Article
- Understanding single-molecule reactions using nanopore-based techniques.Nature chemistry · 2025Review
- Nanopore-based enzyme-linked immunosorbent assay for cancer biomarker detection.Nature nanotechnology · 2025Article
- Nanopore Environmental Analysis.JACS Au · 2025Review
- Nanopore sensing of protein and peptide conformation for point-of-care applications.Nature communications · 2025Review
- Nanopore approaches for single-molecule temporal omics: promises and challenges.Nature methods · 2025Review
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- Tracking flaviviral protease conformational dynamics by tuning single-molecule nanopore tweezers.Biophysical journal · 2025Article
- Allostery can convert binding free energies into concerted domain motions in enzymes.Nature communications · 2024Article
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- Localization and discrimination of GG mismatch in duplex DNA by synthetic ligand-enhanced protein nanopore analysis.Nucleic acids research · 2024Article
- Single-molecule sensing inside stereo- and regio-defined hetero-nanopores.Nature nanotechnology · 2024Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conformational heterogeneity is emerging as a defining characteristic of enzyme function. However, understanding the role of protein conformations requires their thermodynamic and kinetic characterization at the single-molecule level, which remains extremely challenging. Here we report the ligand-induced conformational changes of dihydrofolate reductase (DHFR) by measuring the modulation of the nanopore currents. The long observation time of the electrical recordings enabled the detection of rare conformational transitions hidden in ensemble measurements. We show that DHFR exists in at least four ground-state configurations or conformers with different affinities for its ligands. Unliganded DHFR adopted low-affinity conformers, whereas the binding of substrates promoted the switch to the high-affinity conformer. Conversion between the conformers was accelerated by molecules that stabilized the transition state of DHFR, which suggests that the reaction lowers the energy barrier for conformer exchange and thus facilitates product release. This mechanism might be a general feature in enzymatic reactions affected by product inhibition or when the release of products is the rate-limiting step.
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