ArticleJournal of the American Chemical Society2016
Base Flipping within the α-Hemolysin Latch Allows Single-Molecule Identification of Mismatches in DNA.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Localization and discrimination of GG mismatch in duplex DNA by synthetic ligand-enhanced protein nanopore analysis.Nucleic acids research · 2024Article
- Nanopore sensing: A physical-chemical approach.Biochimica et biophysica acta. Biomembranes · 2021Review
- Stochasticity in Single-Entity Electrochemistry.Current opinion in electrochemistry · 2021Article
- Snapshotting the transient conformations and tracing the multiple pathways of single peptide folding using a solid-state nanopore.Chemical science · 2021Article
- Nanoelectrochemistry in the study of single-cell signaling.Analytical and bioanalytical chemistry · 2020Review
- γ-Hemolysin Nanopore Is Sensitive to Guanine-to-Inosine Substitutions in Double-Stranded DNA at the Single-Molecule Level.Journal of the American Chemical Society · 2018Article
- Nanoscale electrochemical kinetics & dynamics: the challenges and opportunities of single-entity measurements.Faraday discussions · 2018Article
- Single-Molecule Titration in a Protein Nanoreactor Reveals the Protonation/Deprotonation Mechanism of a C:C Mismatch in DNA.Journal of the American Chemical Society · 2018Article
- Membrane protein-based biosensors.Journal of the Royal Society, Interface · 2018Review
- Electro-osmotic capture and ionic discrimination of peptide and protein biomarkers with FraC nanopores.Nature communications · 2017Article
- Label-Free and Real-Time Detection of Protein Ubiquitination with a Biological Nanopore.ACS nano · 2017Article
- Selective single molecule nanopore sensing of proteins using DNA aptamer-functionalised gold nanoparticles.Chemical science · 2017Article
- Interrogation of Base Pairing of the Spiroiminodihydantoin Diastereomers Using the α-Hemolysin Latch.Biochemistry · 2017Article
- Dynamics of a DNA Mismatch Site Held in Confinement Discriminate Epigenetic Modifications of Cytosine.Journal of the American Chemical Society · 2017Article
- Nanopore Sensing.Analytical chemistry · 2017Review
- Kinetics of T3-DNA Ligase-Catalyzed Phosphodiester Bond Formation Measured Using the α-Hemolysin Nanopore.ACS nano · 2016Article
- Energetics of base flipping at a DNA mismatch site confined at the latch constriction of α-hemolysin.Faraday discussions · 2016Article
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5 authors.
Funding
Abstract
A method for identifying and differentiating DNA duplexes containing the mismatched base pairs CC and CA at single molecule resolution with the protein pore α-hemolysin (αHL) is presented. Unique modulating current signatures are observed for duplexes containing the CC and CA mismatches when the mismatch site in the duplex is situated in proximity to the latch constriction of αHL during DNA residence inside the pore. The frequency and current amplitude of the modulation states are dependent on the mismatch type (CC or CA) permitting easy discrimination of these mismatches from one another, and from a fully complementary duplex that exhibits no modulation. We attribute the modulating current signatures to base flipping and subsequent interaction with positively charged lysine residues at the latch constriction of αHL. Our hypothesis is supported by the extended residence times of DNA duplexes within the pore when a mismatch is in proximity to the latch constriction, and by the loss of the two-state current signature in low pH buffers (<6.3), where the protonation of one of the cytosine bases increases the stability of the intrahelical state.
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