{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Piovesana S"],"funding":["European Research Council","Sapienza Universit? di Roma"],"pagination":["9234-9241"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9260711"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["94(26)"],"pubmed_abstract":["Site localization of protein sulfation by high-throughput proteomics remains challenging despite the technological improvements. In this study, sequence analysis and site localization of sulfation in tryptic peptides were determined under a conventional nano-liquid chromatography-mass spectrometry configuration. Tryptic sulfopeptide standards were used to study different fragmentation strategies, including collision-induced dissociation (CID), higher-energy collisional dissociation (HCD), electron-transfer dissociation (ETD), electron-transfer/higher-energy collision dissociation (EThcD), and electron-transfer/collision-induced dissociation (ETciD), in the positive ionization mode. Sulfopeptides displayed only neutral loss of SO<sub>3</sub> under CID, while the sequence could be determined"],"journal":["Analytical chemistry"],"pubmed_title":["The Key Role of Metal Adducts in the Differentiation of Phosphopeptide from Sulfopeptide Sequences by High-Resolution Mass Spectrometry."],"pmcid":["PMC9260711"],"funding_grant_id":["AR220172B85F20D6","823839"],"pubmed_authors":["Cerrato A","Lagana A","Montone CM","Piovesana S","Zenezini Chiozzi R","Cavaliere C","Capriotti AL"],"additional_accession":[]},"is_claimable":false,"name":"The Key Role of Metal Adducts in the Differentiation of Phosphopeptide from Sulfopeptide Sequences by High-Resolution Mass Spectrometry.","description":"Site localization of protein sulfation by high-throughput proteomics remains challenging despite the technological improvements. In this study, sequence analysis and site localization of sulfation in tryptic peptides were determined under a conventional nano-liquid chromatography-mass spectrometry configuration. Tryptic sulfopeptide standards were used to study different fragmentation strategies, including collision-induced dissociation (CID), higher-energy collisional dissociation (HCD), electron-transfer dissociation (ETD), electron-transfer/higher-energy collision dissociation (EThcD), and electron-transfer/collision-induced dissociation (ETciD), in the positive ionization mode. Sulfopeptides displayed only neutral loss of SO<sub>3</sub> under CID, while the sequence could be determined","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jul","modification":"2025-04-05T14:25:58.229Z","creation":"2022-07-23T09:39:22.488Z"},"accession":"S-EPMC9260711","cross_references":{"pubmed":["35714062"],"doi":["10.1021/acs.analchem.1c05621"]}}