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- W2883681250 abstract "Protein phosphorylation is one of the most ubiquitous post-translational modifications in humans, and trypsin-digested phosphorylated peptides have been analyzed by reversed phase LC/MS using C18-silica columns under acidic conditions to profile human phosphoproteomes. Here, we report that phosphopeptides generally exhibit stronger retention than their unphosphorylated counterparts when C18-silica columns are used with acetic acid or formic acid as an ion-pairing reagent, whereas the retention order is reversed when less hydrophobic stationary phases such as C4-silica columns are employed. Similarly the retention reversal is observed when more hydrophobic ion-pairing reagents such as trifluoroacetic acid are used with C18-silica columns. These phenomena could be explained by the smaller S-values of phosphopeptides in linear solvation strength theory, based on the reduced net charge caused by intramolecular interaction between phosphate and basic groups." @default.
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- W2883681250 date "2018-07-27" @default.
- W2883681250 modified "2023-09-25" @default.
- W2883681250 title "Retention Order Reversal of Phosphorylated and Unphosphorylated Peptides in Reversed-Phase LC/MS" @default.
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- W2883681250 doi "https://doi.org/10.2116/analsci.18scp11" @default.
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