Journal
ANALYTICAL CHEMISTRY
Volume 93, Issue 45, Pages 14946-14954Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.1c00895
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Funding
- Wellcome Trust [WT100093MA]
- EPSRC program [EP/I032517/1]
- EPSRC/DSTL MURI [EP/N018680/1]
- Pathways to Impact grant [EP/K503733/1]
- ERC ASTEX project [290467]
- EPSRC [EP/I032517/1, EP/N018680/1] Funding Source: UKRI
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The study introduces a protein database search engine based on 2D-PC-MS method, which can accurately identify protein sequences by matching theoretical and experimentally detected correlating fragments, with high structural specificity. This search engine is not only suitable for peptide identification, but also for intact protein identification.
We present a protein database search engine for the automatic identification of peptide and protein sequences using the recently introduced method of two-dimensional partial covariance mass spectrometry (2D-PC-MS). Because the 2D-PC-MS measurement reveals correlations between fragments stemming from the same or consecutive decomposition processes, the first-of-its-kind 2D-PC-MS search engine is based entirely on the direct matching of the pairs of theoretical and the experimentally detected correlating fragments, rather than of individual fragment signals or their series. We demonstrate that the high structural specificity afforded by 2D-PC-MS fragment correlations enables our search engine to reliably identify the correct peptide sequence, even from a spectrum with a large proportion of contaminant signals. While for peptides, the 2D-PC-MS correlation-matching procedure is based on complementary and internal ion correlations, the identification of intact proteins is entirely based on the ability of 2D-PC-MS to spatially separate and resolve the experimental correlations between complementary fragment ions.
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