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dc.contributor.authorMcKenzie-Coe, Alan A
dc.contributor.authorJohnson, Danté T
dc.contributor.authorPeacock, Riley B
dc.contributor.authorZhang, Zhihui
dc.contributor.authorJones, Lisa M
dc.date.accessioned2021-07-29T17:38:01Z
dc.date.available2021-07-29T17:38:01Z
dc.date.issued2021-06-25
dc.identifier.urihttp://hdl.handle.net/10713/16258
dc.description.abstractFast photochemical oxidation of proteins (FPOP) has demonstrated the ability to inform on the higher order structure of proteins. Recent technological advances have extended FPOP to live cells (IC-FPOP) using multiple cell lines and in vivo (IV-FPOP) using C. elegans. These innovations allow proteins to be studied in their native cellular environment. Hydroxyl radicals are generated via the photoloysis of hydrogen peroxide. Hydrogen peroxide is a signaling molecule that can induce changes to some proteins in the cell limiting the proteins that can be studied by IC-FPOP. Here, we evaluate the sulfate radical anion as a footprinting label in IC-FPOP with sodium persulfate as the precursor. Our findings show a 1.5-fold increase in the number of modified proteins compared to IC-FPOP using hydroxyl radicals at the same precursor concentration demonstrating the amenability of this radical with IC-FPOP.en_US
dc.description.urihttps://doi.org/10.1021/jasms.1c00038en_US
dc.language.isoenen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.ispartofJournal of the American Society for Mass Spectrometryen_US
dc.subjecthydroxylsen_US
dc.subjectmodificationen_US
dc.subjectanionsen_US
dc.subjectpeptides and proteinsen_US
dc.subjectmonomersen_US
dc.titleEvaluating the Sulfate Radical Anion as a New Reagent for In-Cell Fast Photochemical Oxidation of Proteinsen_US
dc.typeArticleen_US
dc.identifier.doi10.1021/jasms.1c00038
dc.identifier.pmid34170666
dc.source.volume32
dc.source.issue7
dc.source.beginpage1644
dc.source.endpage1647
dc.source.countryUnited States


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