Open AccessGlobal Identification of Protein Post-translational Modifications in a Single-Pass Database Search
Author(s) -
Michael R. Shortreed,
Craig D. Wenger,
Brian L. Frey,
Gloria Sheynkman,
Mark Scalf,
Mark P. Keller,
Alan D. Attie,
Lloyd M. Smith
Publication year - 2015
Publication title -
journal of proteome research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.644
H-Index - 161
eISSN - 1535-3907
pISSN - 1535-3893
DOI - 10.1021/acs.jproteome.5b00599
Subject(s) - database search engine , identification (biology) , posttranslational modification , computer science , proteomics , database , computational biology , search engine , information retrieval , biology , genetics , biochemistry , botany , gene , enzyme
Bottom-up proteomics database search algorithms used for peptide identification cannot comprehensively identify post-translational modifications (PTMs) in a single-pass because of high false discovery rates (FDRs). A new approach to database searching enables global PTM (G-PTM) identification by exclusively looking for curated PTMs, thereby avoiding the FDR penalty experienced during conventional variable modification searches. We identified over 2200 unique, high-confidence modified peptides comprising 26 different PTM types in a single-pass database search.