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Updated: Aug 24, 2026

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
Published on: March 23, 2020
Isomeric discrimination of arginine-containing dipeptides using electrospray ionization-ion trap mass spectrometry
Kevin A Schug1, Wolfgang Lindner, Karel Lemr
1Department of Analytical Chemistry, University of Vienna, Vienna, Austria.
Abstract:
The Kinetic Method (KM), applied commonly for thermochemical determinations, is used here for sterically-controlled isomeric determination of N- versus C-terminal Arg-containing dipeptide isomers (ArgX versus XArg; where X = His, Leu, Lys, Pro, Ser, Phe, and Tyr). The KM is offered as an alternate approach to direct collision-induced dissociation (CID) procedures. Through formation, isolation, and dissociation of a sterically-encumbered, metal-centered complex with electrospray ionization ion trap mass spectrometry technology, reference dipeptide molecules are screened to quantitatively differentiate a mixture of isomers based on their arrangement about the metal center. Arg-containing dipeptide molecules are chosen because of their contribution in a wide array of protein and peptide functions. Additionally, problems cited previously for evaluation of systems containing Arg residues (due to the incorporation of the guanidinium moiety) by the KM are addressed. The method is shown to be successful for highlighting favorable reference analytes (e.g., ArgPhe, ArgLeu, ProArg, PheArg, among others) for exceptional discrimination (R(iso) > 2.0) of the majority of N- and C-terminal Arg-containing peptides tested.
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