ArticleNature nanotechnology2016
Reading the primary structure of a protein with 0.07 nm
Article in Nature nanotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
71 citing papers in PubMed, 189 citations in OpenAlex.
- Article
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- Mechanisms of Adeno-Associated Virus Serotype 9 Vector Characterization and Quality Control through Solid-State Nanopores.ACS nano · 2026Article
- NanoSSL: attention mechanism-based self-supervised learning method for protein identification using nanopores.Bioinformatics (Oxford, England) · 2026Article
- The Potential of Nanopore Technologies in Peptide and Protein Sensing for Biomarker Detection.Biosensors · 2025Review
- Vectorial Discrimination of Small Molecules with a Macrocycle Adaptor-Protein Nanopore System and Nanocavity-Dependent, pH Gradient-Controlled Analyte Kinetics.Analytical chemistry · 2025Article
- Graphene Nanopore Fabrication and Applications.International journal of molecular sciences · 2025Review
- Localized Nanopore Fabrication in Silicon Nitride Membranes by Femtosecond Laser Exposure and Subsequent Controlled Breakdown.ACS applied materials & interfaces · 2025Article
- The Road Toward Nanopore Sequencing of Glycosaminoglycans.Handbook of experimental pharmacology · 2025Review
- Article
- Electro-osmotic Flow Generation via a Sticky Ion Action.ACS nano · 2024Article
- Integrated In-Plane Nanofluidic Devices for Resistive-Pulse Sensing.Annual review of analytical chemistry (Palo Alto, Calif.) · 2024Review
- Nanopore DNA sequencing technologies and their applications towards single-molecule proteomics.Nature chemistry · 2024Review
- Article
- Molecular Determinants of Current Blockade Produced by Peptide Transport Through a Nanopore.ACS nanoscience Au · 2024Review
- Peptide sequencing based on host-guest interaction-assisted nanopore sensing.Nature methods · 2024Article
- Electro-Osmotic Flow Generation via a Sticky Ion Action.bioRxiv : the preprint server for biology · 2023Article
- Molecular sensitised probe for amino acid recognition within peptide sequences.Nature communications · 2023Article
- Review
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The primary structure of a protein consists of a sequence of amino acids and is a key factor in determining how a protein folds and functions. However, conventional methods for sequencing proteins, such as mass spectrometry and Edman degradation, suffer from short reads and lack sensitivity, so alternative approaches are sought. Here, we show that a subnanometre-diameter pore, sputtered through a thin silicon nitride membrane, can be used to detect the primary structure of a denatured protein molecule. When a denatured protein immersed in electrolyte is driven through the pore by an electric field, measurements of a blockade in the current reveal nearly regular fluctuations, the number of which coincides with the number of residues in the protein. Furthermore, the amplitudes of the fluctuations are highly correlated with the volumes that are occluded by quadromers (four residues) in the primary structure. Each fluctuation, therefore, represents a read of a quadromer. Scrutiny of the fluctuations reveals that the subnanometre pore is sensitive enough to read the occluded volume that is related to post-translational modifications of a single residue, measuring volume differences of ∼0.07 nm
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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.