Link to the University of Pittsburgh Homepage
Link to the University Library System Homepage Link to the Contact Us Form

Multiple proteases to localize oxidation sites

Gu, L and Robinson, RAS (2015) Multiple proteases to localize oxidation sites. PLoS ONE, 10 (3).

Published Version
Available under License : See the attached license file.

Download (2MB)
[img] Plain Text (licence)
Available under License : See the attached license file.

Download (1kB)


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.


Social Networking:
Share |


Item Type: Article
Status: Published
CreatorsEmailPitt UsernameORCID
Gu, Llig32@pitt.eduLIG32
Robinson, RAS
ContributionContributors NameEmailPitt UsernameORCID
Date: 16 March 2015
Date Type: Publication
Journal or Publication Title: PLoS ONE
Volume: 10
Number: 3
DOI or Unique Handle: 10.1371/journal.pone.0116606
Schools and Programs: Dietrich School of Arts and Sciences > Chemistry
Refereed: Yes
PubMed ID: 25775238
Date Deposited: 12 May 2015 19:53
Last Modified: 30 Mar 2021 16:55


Monthly Views for the past 3 years

Plum Analytics

Actions (login required)

View Item View Item