A turn-key approach for large-scale identification of complex posttranslational modifications.
Ontology highlight
ABSTRACT: The conjugation of complex post-translational modifications (PTMs) such as glycosylation and Small Ubiquitin-like Modification (SUMOylation) to a substrate protein can substantially change the resulting peptide fragmentation pattern compared to its unmodified counterpart, making current database search methods inappropriate for the identification of tandem mass (MS/MS) spectra from such modified peptides. Traditionally it has been difficult to develop new algorithms to identify these atypical peptides because of the lack of a large set of annotated spectra from which to learn the altered fragmentation pattern. Using SUMOylation as an example, we propose a novel approach to generate large MS/MS training data from modified peptides and derive an algorithm that learns properties of PTM-specif
SUBMITTER: Wang J
PROVIDER: S-EPMC3993922 | biostudies-literature | 2014 Mar
REPOSITORIES: biostudies-literature
ACCESS DATA