Recent advances in top-down mass spectrometry enabled identification ofintact proteins, but this technology still faces challenges. For example,top-down mass spectrometry suffers from a lack of sensitivity since the ioncounts for a single fragmentation event are often low. In contrast, nanoporetechnology is exquisitely sensitive to single intact molecules, but it has onlybeen successfully applied to DNA sequencing, so far. Here, we explore thepotential of sub-nanopores for single-molecule protein identification (SMPI)and describe an algorithm for identification of the electrical current blockadesignal (nanospectrum) resulting from the translocation of a denaturated,linearly charged protein through a sub-nanopore. The analysis of identificationp-values suggests that the current technology is already sufficient formatching nanospectra against small protein databases, e.g., proteinidentification in bacterial proteomes.
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