Yang: Site-specific mapping and quantification of protein S-sulfenylation in cells

ABSTRACT: The files in this archive represent the supporting data for "Site-specific mapping and quantification of protein S-sulfenylation in cells," a paper to appear in Nature Communications (2014). The authors are Jing Yang, Vinayak Gupta, Kate S. Carroll, and Daniel C. Liebler, working at Vanderbilt University School of Medicine in Nashville, TN, and The Scripps Research Institute, Jupiter, FL. Human cell lines were treated with an alkynyl probe to label S-sulfenylcysteines and the labeled proteins were tagged with an azidobiotin reagent by click chemistry, digested with trypsin, and desalted (described in the paper in detail). Peptide capture was accomplished through streptavidin columns. Data-dependent LC-MS/MS experiments without prior fractionation were conducted on a Thermo Q-Exactive, employing HCD fragmentation. Light and heavy variants of each peptide would carry 333.1689 Da and 339.2065 Da mass shifts on Cysteines, respectively, and iodoacetamide would modify remaining cysteines by 57.021464 Da.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Daniel C. Liebler 

PROVIDER: MSV000078777 | MassIVE | Thu Jul 10 13:02:00 BST 2014

REPOSITORIES: MassIVE