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Analysis of Glutamine Deamidation: Products, Pathways, and Kinetics
preprintsubmitted on 10.07.2019, 16:44 and posted on 11.07.2019, 13:15 by Dylan L. Riggs, Jacob W. Silzel, Yana A. Lyon, Amrik S. Kang, Ryan Julian
This manuscript examines glutamine deamidation, which is a spontaneous chemical modification similar to the much more thoroughly characterized asparagine deamidation. Although both processes share similarities and are known to occur in long-lived proteins, here we establish that important differences exist as well. For example, the distribution of isomers generated following glutamine deamidation contains far fewer D-residues. Furthermore, with the exception of QG motifs, glutamine deamidation occurs primarily by direct hydrolysis and produces less isoglutamic acid as a result. In addition, we demonstrate that radical-directed dissociation generates abundant, characteristic, fragment ions that can be used to easily distinguish glutamic acid from isoglutamic acid.
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in Analytical Chemistry
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