Peptide sequence motif analysis of tandem MS data with the SALSA algorithm
| Autor: | Daniel E. Mason, Laura Tiscareno, Beau T. Hansen, Daniel C. Liebler, Sean Davey |
|---|---|
| Rok vydání: | 2002 |
| Předmět: |
Amino Acid Motifs
Peptide Target peptide Mass Spectrometry Analytical Chemistry Sequence Analysis Protein medicine Animals Humans Bovine serum albumin Peptide sequence computer.programming_language chemistry.chemical_classification Chromatography biology Tandem Human serum albumin chemistry Proteome biology.protein Peptides Algorithm computer SALSA Algorithms medicine.drug |
| Zdroj: | Analytical chemistry. 74(1) |
| ISSN: | 0003-2700 |
| Popis: | We have developed a pattern recognition algorithm called SALSA (scoring algorithm for spectral analysis) for the detection of specific features in tandem MS (MS-MS) spectra. Application of the SALSA algorithm to the detection of peptide MS-MS ion series enables identification of MS-MS spectra displaying characteristics of specific peptide sequences. SALSA analysis scores MS-MS spectra based on correspondence between theoretical ion series for peptide sequence motifs and actual MS-MS product ion series, regardless of their absolute positions on the m/z axis. Analyses of tryptic digests of bovine serum albumin (BSA) by LC-MS-MS followed by SALSA analysis detected MS-MS spectra for both unmodified and multiple modified forms of several BSA tryptic peptides. SALSA analysis of MS-MS data from mixtures of BSA and human serum albumin (HSA) tryptic digests indicated that ion series searches with BSA peptide sequence motifs identified MS-MS spectra for both BSA and closely related HSA peptides. Optimal discrimination between MS-MS spectra of variant peptide forms is achieved when the SALSA search criteria are optimized to the target peptide. Application of SALSA to LC-MS-MS proteome analysis will facilitate the characterization of modified and sequence variant proteins. |
| Databáze: | OpenAIRE |
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