{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Cheng Z"],"funding":["National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["18017-18024"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9912381"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["94(51)"],"pubmed_abstract":["Protein posttranslational modifications (PTMs) are key modulators of protein structure and function that often change in a dynamic fashion in response to cellular stimuli. Dynamic PTMs are very challenging to structurally characterize using modern techniques, including covalent labeling methods, due to the presence of multiple proteoforms and conformers together in solution. We have coupled an ion exchange high-performance liquid chromatography separation with a flash oxidation system [ion exchange chromatography liquid chromatography-flash oxidation (IEX LC-FOX)] to successfully elucidate structural changes among three phosphoproteoforms of ovalbumin (OVA) during dephosphorylation with alkaline phosphatase. Real-time dosimetry indicates no difference in the effective radical dose between "],"journal":["Analytical chemistry"],"pubmed_title":["Structural Analysis of Phosphorylation Proteoforms in a Dynamic Heterogeneous System Using Flash Oxidation Coupled In-Line with Ion Exchange Chromatography."],"pmcid":["PMC9912381"],"funding_grant_id":["R01 GM127267","R01GM127267","P20 GM130460"],"pubmed_authors":["Sharp JS","Misra SK","Shami A","Cheng Z"],"additional_accession":[]},"is_claimable":false,"name":"Structural Analysis of Phosphorylation Proteoforms in a Dynamic Heterogeneous System Using Flash Oxidation Coupled In-Line with Ion Exchange Chromatography.","description":"Protein posttranslational modifications (PTMs) are key modulators of protein structure and function that often change in a dynamic fashion in response to cellular stimuli. Dynamic PTMs are very challenging to structurally characterize using modern techniques, including covalent labeling methods, due to the presence of multiple proteoforms and conformers together in solution. We have coupled an ion exchange high-performance liquid chromatography separation with a flash oxidation system [ion exchange chromatography liquid chromatography-flash oxidation (IEX LC-FOX)] to successfully elucidate structural changes among three phosphoproteoforms of ovalbumin (OVA) during dephosphorylation with alkaline phosphatase. Real-time dosimetry indicates no difference in the effective radical dose between ","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-05-28T13:20:18.144Z","creation":"2025-04-04T03:00:41.544Z"},"accession":"S-EPMC9912381","cross_references":{"pubmed":["36512753"],"doi":["10.1021/acs.analchem.2c04365"]}}