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Single-molecule identification of full-length proteins with single-amino-acid resolution using nanopores

Bonini, A.; Lu, C.; Mantovanelli, L.; Versloot, R. C. A.; Jansen, A.; O Connell Stack, P.; Tsousi, V.; Knecht, P.; Lang, K.; Heron, A.; Maglia, G.

2026-01-08 biophysics
10.64898/2026.01.08.698148 bioRxiv
Show abstract

Nanopore-based technologies show promise in single-molecule protein sequencing. By using an unfoldase and a nanopore with enhanced electroosmotic flow, here we show the continuous identification of generic proteins during single nanopore passes. This approach enables the recording of differences in charge and size from single amino acid substitutions compared to reference signals, paving the way for single-molecule protein sequencing and high-throughput proteomics.

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"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.