Authors
John R Yates, Jimmy K Eng, Ashley L McCormack, David Schieltz
Publication date
1995/4/1
Journal
Analytical chemistry
Volume
67
Issue
8
Pages
1426-1436
Publisher
American Chemical Society
Description
A method to correlate uninterpreted tandem mass spectra of modified peptides, produced under low-energy (10-50 eV) collision conditions, with amino acid sequences in a protein database has been developed. The fragmen-tation patterns observed in the tandem mass spectra of peptides containing covalent modifications is used to directly search and fit linear amino acid sequences in the database. Specific information relevant to sites of modification is not contained in the character-based sequence information of the databases. The search method consid-ers each putative modification site as both modified and unmodified in one pass through the database andsimul-taneously considers up to three different sites of modifica-tion. The search method will identify the correct sequence if the tandem mass spectrum did not represent a modified peptide. This approach is demonstrated with peptides containing …
Total citations
19951996199719981999200020012002200320042005200620072008200920102011201220132014201520162017201820192020202120222023202461930393252385855551021181048795921029781555344312730242020612