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Sequit: software for de novo peptide sequencing by matrix‐assisted laser desorption/ionization post‐source decay mass spectrometry
Author(s) -
Demine Rodion,
Walden Peter
Publication year - 2004
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1420
Subject(s) - chemistry , mass spectrometry , peptide , proteomics , matrix assisted laser desorption/ionization , peptide mass fingerprinting , protein mass spectrometry , bottom up proteomics , mass spectrum , matrix (chemical analysis) , database search engine , computational biology , chromatography , peptide sequence , combinatorial chemistry , database , desorption , tandem mass spectrometry , biochemistry , information retrieval , computer science , search engine , gene , adsorption , biology
Abstract Peptide sequencing by mass spectrometry is gaining increasing importance for peptide chemistry and proteomics. However, available tools for interpreting matrix‐assisted laser desorption/ionization post‐source decay (MALDI‐PSD) mass spectra depend on databases, and identify peptides by matching experimental data with spectra calculated from database sequences. This severely obstructs the identification of proteins and peptides not listed in databases or of variations, e.g. mutated proteins. The development of a new computer program for database‐independent peptide sequencing by MALDI‐PSD mass spectrometry is reported here. This computer program was validated by the determination of the correct sequences for various peptides including sequences listed in the sequence databases, but also for peptides that deviate from database sequences or are completely artificial. This strategy should substantially facilitate the identification of novel or variant peptides and proteins, and increase the power of MALDI‐PSD analyses in proteomics. Copyright © 2004 John Wiley & Sons, Ltd.