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Mapping phosphorylation post-translational modifications along single peptides with nanopores

Nova, I. C.; Ritmejeris, J.; Brinkerhoff, H.; Koenig, T. J. R.; Gundlach, J. H.; Dekker, C.

2022-11-12 biophysics
10.1101/2022.11.11.516163 bioRxiv
Show abstract

Current methods to detect post-translational modifications (PTMs) of proteins, such as phosphate groups, cannot measure single molecules and often cannot differentiate between closely spaced phosphorylation sites. Using a nanopore sequencing approach, we here report detection of PTMs at the single-molecule level on immunopeptide sequences with cancer-associated phosphate variants. We reliably discriminate peptide sequences with one or two closely spaced phosphates with 95% accuracy for individual reads of single molecules.

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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.