ArticleBiochemistry2017
Aberrantly Large Single-Channel Conductance of Polyhistidine Arm-Containing Protein Nanopores.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed.
- Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025Article
- Review
- Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021Review
- Protein Ligand-Induced Amplification in the 1/Langmuir : the ACS journal of surfaces and colloids · 2020Article
- Single-Molecule Protein Detection in a Biofluid Using a Quantitative Nanopore Sensor.ACS sensors · 2019Article
- High-Throughput Screening of Protein-Detergent Complexes Using Fluorescence Polarization Spectroscopy.Current protocols in protein science · 2019Article
- Article
- Real-time measurement of protein-protein interactions at single-molecule resolution using a biological nanopore.Nature biotechnology · 2018Article
- Kinetics of Membrane Protein-Detergent Interactions Depend on Protein Electrostatics.The journal of physical chemistry. B · 2018Article
- Detergent Desorption of Membrane Proteins Exhibits Two Kinetic Phases.The journal of physical chemistry letters · 2018Article
- Understanding antibiotic resistance via outer membrane permeability.Infection and drug resistance · 2018Review
- Quantification of Membrane Protein-Detergent Complex Interactions.The journal of physical chemistry. B · 2017Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
There have been only a few studies reporting on the impact of polyhistidine affinity tags on the structure, function, and dynamics of proteins. Because of the relatively short size of the tags, they are often thought to have little or no effect on the conformation or activity of a protein. Here, using membrane protein design and single-molecule electrophysiology, we determined that the presence of a hexahistidine arm at the N-terminus of a truncated FhuA-based protein nanopore, leaving the C-terminus untagged, produces an unusual increase in the unitary conductance to ∼8 nS in 1 M KCl. To the best of our knowledge, this is the largest single-channel conductance ever recorded with a monomeric β-barrel outer membrane protein. The hexahistidine arm was captured by an anti-polyhistidine tag monoclonal antibody added to the side of the channel-forming protein addition, but not to the opposite side, documenting that this truncated FhuA-based protein nanopore inserts into a planar lipid bilayer with a preferred orientation. This finding is in agreement with the protein insertion in vivo, in which the large loops face the extracellular side of the membrane. The aberrantly large single-channel conductance, likely induced by a greater cross-sectional area of the pore lumen, along with the vectorial insertion into a lipid membrane, will have profound implications for further developments of engineered protein nanopores.
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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 Socratic graph.