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Mol Cell Proteomics. 2008 Dec;7(12):2386-98. doi: 10.1074/mcp.M800021-MCP200. Epub 2008 Jul 24.

In-depth analysis of tandem mass spectrometry data from disparate instrument types.

Author information

  • 1Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158-2517, USA. chalkley@cgl.ucsf.edu

Abstract

Mass spectrometric analyses of protein digests produce large numbers of fragmentation spectra that are not identified by routine database searching strategies. Some of these spectra could be identified by development of improved search engines. However, many of these spectra represent fragmentation of peptide components bearing modifications that are not routinely considered in database searches. Here we present new software within Protein Prospector that allows comprehensive analysis of data sets by analyzing the data at increasing levels of depth. Analysis of published data sets is presented to illustrate that the software is not biased to any instrument types. The results show that these data sets contain many modified peptides. As well as searching for known modification types, Protein Prospector permits the detection and identification of unexpected or novel modifications by searching for any mass shift within a user-specified mass range to any chosen amino acid(s). Several modifications never previously reported in proteomics data were identified in these standard data sets using this mass modification searching approach.

PMID:
18653769
[PubMed - indexed for MEDLINE]
PMCID:
PMC2596346
Free PMC Article
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