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Quantitative Proteomics Using Reductive Dimethylation for Stable Isotope Labeling
Published on: July 1, 2014
Rapid diazotransfer for selective lysine labelling
Susannah H Calvert1,2, Tomasz Pawlak1, Gary Hessman1
1School of Chemistry, Trinity Biomedical Science Institute, Trinity College Dublin, D02 R590, Ireland. jmcgoura@tcd.ie.
Abstract:
Azide functionalization of protein and peptide lysine residues allows selective bioorthogonal labeling to introduce new, site selective functionaltiy into proteins. Optimised diazotransfer reactions under mild conditions allow aqueous diazotransfer to occur in just 20 min at pH 8.5 on amino acid, peptide and protein targets. In addition, conditons can be modified to selectively label a single lysine residue in both protein targets investigated. Finally, we demonstrate selective modification of proteins containing a single azidolysine using copper(I)-catalyzed triazole formation.
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