ArticleiScience2021
Evaluation of FRET X for single-molecule protein fingerprinting.
Article in iScience, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 25 citations in OpenAlex.
- Label-Free Optical Differentiation of Single Diffusing Amino Acids at Picomolar Concentrations.Research square · 2026Article
- Amplifiable protein identification via residue-resolved barcoding and composition code counting.National science review · 2024Article
- Topographic fingerprinting of single proteins and proteoforms.Nature nanotechnology · 2024Article
- Full-length single-molecule protein fingerprinting.Nature nanotechnology · 2024Article
- Real-time detection of 20 amino acids and discrimination of pathologically relevant peptides with functionalized nanopore.Nature methods · 2024Article
- Recent methodological advances towards single-cell proteomics.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2023Review
- Robust and scalable single-molecule protein sequencing with fluorosequencing.bioRxiv : the preprint server for biology · 2023Article
- Review
- Single-Molecule Peptide Identification Using Fluorescence Blinking Fingerprints.Journal of the American Chemical Society · 2023Article
- Article
- Protein Sequencing, One Molecule at a Time.Annual review of biophysics · 2022Review
- Herding cats: Label-based approaches in protein translocation through nanopore sensors for single-molecule protein sequence analysis.iScience · 2021Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Single-molecule protein identification is an unrealized concept with potentially ground-breaking applications in biological research. We propose a method called FRET X (Förster Resonance Energy Transfer via DNA eXchange) fingerprinting, in which the FRET efficiency is read out between exchangeable dyes on protein-bound DNA docking strands and accumulated FRET efficiencies constitute the fingerprint for a protein. To evaluate the feasibility of this approach, we simulated fingerprints for hundreds of proteins using a coarse-grained lattice model and experimentally demonstrated FRET X fingerprinting on model peptides. Measured fingerprints are in agreement with our simulations, corroborating the validity of our modeling approach. In a simulated complex mixture of >300 human proteins of which only cysteines, lysines, and arginines were labeled, a support vector machine was able to identify constituents with 95% accuracy. We anticipate that our FRET X fingerprinting approach will form the basis of an analysis tool for targeted proteomics.
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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.