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A novel multifunctional labeling reagent for enhanced protein characterization with mass spectrometry
Author(s) -
Peters Eric C.,
Horn David M.,
Tully David C.,
Brock Ansgar
Publication year - 2001
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.517
Subject(s) - chemistry , lysine , mass spectrometry , reagent , peptide , chromatography , deuterium , mass spectrum , imidazole , peptide mapping , isotopic labeling , isobaric labeling , tandem mass spectrometry , derivatization , combinatorial chemistry , protein mass spectrometry , amino acid , stereochemistry , peptide sequence , organic chemistry , biochemistry , physics , quantum mechanics , gene
Individual peptides with lysine at the C‐terminus as well as protein tryptic digests were reacted with 2‐methoxy‐4,5‐dihydro‐1 H ‐imidazole, converting lysine residues to their 4,5‐dihydro‐1 H ‐imidazol‐2‐yl derivatives. The mass spectra of derivatized digests exhibit a greater number of more intense features than their underivatized counterparts, thus increasing the information obtained in peptide mapping experiments. Additionally, MS/MS spectra of the derivatized peptides are greatly simplified in comparison to their native species, yielding primarily an easily interpretable series of y‐ions. Finally, this novel label also enables differential quantitation studies, as a stable isotopic form containing four deuterium atoms can readily be produced. Copyright © 2001 John Wiley & Sons, Ltd.