Electron Capture vs. Transfer Dissociation for Site Determination of Tryptic Peptide Tyrosine Sulfation: Direct Detection of Fibrinogen Sulfation Sites and Identification of Novel Isobaric Interferences

ABSTRACT: Tyrosine sulfation is an understudied posttranslational modification (PTM) of crucial biological significance. Conventional liquid chromatography-tandem mass spectrometry (LC-MS/MS) methods are unable to directly identify sulfation sites due to the high lability of the sulfate PTM. In this study, we were able to directly detect and localize tyrosine sulfation sites in a proteomics workflow. To meet that objective, we combined bottom-up nanoflow LC-beam-type CID (nanoLC-HCD) with conventional “MSFragger-Labile” analysis, nanoLC-electron transfer with supplemental HCD (EThcD) MS/MS, and LC-electron capture dissociation (ECD) MS/MS for the characterization of bovine fibrinogen sulfopeptide candidates from both purified protein and from plasma.

INSTRUMENT(S): Orbitrap Fusion Lumos, Bruker Daltonics solarix series

ORGANISM(S): Bos Taurus (bovine)

SUBMITTER: Menatallah Youssef  

LAB HEAD: Kristina Hakansson

PROVIDER: PXD048811 | Pride | 2024-06-21

REPOSITORIES: Pride