relation: http://d-scholarship-dev.library.pitt.edu/24104/
title: Multiple proteases to localize oxidation sites
creator: Gu, L
creator: Robinson, RAS
description: Proteins present in cellular environments with high levels of reactive oxygen and nitrogen species and/or low levels of antioxidants are highly susceptible to oxidative post-translational modification (PTM). Irreversible oxidative PTMs can generate a complex distribution of modified protein molecules, recently termed as proteoforms. Using ubiquitin as a model system, we mapped oxidative modification sites using trypsin, Lys-C, and Glu-C peptides. Several M+16 Da proteoforms were detected as well as proteoforms that include other previously unidentified oxidative modifications. This work highlights the use of multiple protease digestions to give insights to the complexity of oxidative modifications possible in bottom-up analyses.
date: 2015-03-16
type: Article
type: PeerReviewed
format: application/pdf
language: en
rights: attached
identifier: http://d-scholarship-dev.library.pitt.edu/24104/1/journal.pone.0116606.pdf
format: text/plain
language: en
rights: attached
identifier: http://d-scholarship-dev.library.pitt.edu/24104/4/licence.txt
identifier:   Gu, L and Robinson, RAS  (2015) Multiple proteases to localize oxidation sites.  PLoS ONE, 10 (3).       
relation: 10.1371/journal.pone.0116606