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- W3203203247 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." @default.
- W3203203247 created "2021-10-11" @default.
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- W3203203247 date "2021-11-01" @default.
- W3203203247 modified "2023-10-11" @default.
- W3203203247 title "Evaluation of FRET X for single-molecule protein fingerprinting" @default.
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- W3203203247 doi "https://doi.org/10.1016/j.isci.2021.103239" @default.
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