ArticleThe journal of physical chemistry letters2014
Effect of an Electrolyte Cation on Detecting DNA Damage with the Latch Constriction of α-Hemolysin.
Article in The journal of physical chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Analytical and Structural Studies for the Investigation of Oxidative Stress in Guanine Oligonucleotides.International journal of molecular sciences · 2020Review
- Biomimetic Membranes with Transmembrane Proteins: State-of-the-Art in Transmembrane Protein Applications.International journal of molecular sciences · 2019Review
- Nanoscale electrochemical kinetics & dynamics: the challenges and opportunities of single-entity measurements.Faraday discussions · 2018Article
- Interference-Free Detection of Genetic Biomarkers Using Synthetic Dipole-Facilitated Nanopore Dielectrophoresis.ACS nano · 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
- Base Flipping within the α-Hemolysin Latch Allows Single-Molecule Identification of Mismatches in DNA.Journal of the American Chemical Society · 2016Article
- Unzipping of A-Form DNA-RNA, A-Form DNA-PNA, and B-Form DNA-DNA in the α-Hemolysin Nanopore.Biophysical journal · 2016Article
- Characterization of Interstrand DNA-DNA Cross-Links Using the α-Hemolysin Protein Nanopore.ACS nano · 2015Article
- Differentiation of G:C vs A:T and G:C vs G:mC Base Pairs in the Latch Zone of α-Hemolysin.ACS nano · 2015Article
- Challenges in DNA motion control and sequence readout using nanopore devices.Nanotechnology · 2015Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The effect of an electrolyte cation on the unzipping of furan-containing double-stranded DNA in an α-hemolysin (αHL) nanopore is described. The current through an open αHL channel increases in proportion to the ion mobility. However, the ionic current measured during residence of a DNA duplex inside of the protein pore shows a more complex dependence on the choice of cation, indicating that the current measured during DNA residence in the pore is modulated by the specific interactions of the cations with the DNA and/or αHL. The residence time (stability) of the DNA duplex inside of the pore prior to unzipping is also highly dependent on the cation, in striking contrast to the small variation in duplex stability (as measured by the melting temperature) in bulk electrolyte solution. A missing base in DNA can be detected in the latch region of αHL with optimal current resolution in RbCl, while optimal time resolution is possible in LiCl.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.