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Analysis of Glutamine Deamidation: Products, Pathways, and Kinetics

preprint
submitted 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.

Funding

Identification of peptide epimers in crystallin proteins

National Institute of General Medical Sciences

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History

Email Address of Submitting Author

ryan.julian@ucr.edu

Institution

University of California, Riverside

Country

United States

ORCID For Submitting Author

0000-0003-1580-8355

Declaration of Conflict of Interest

no conflict of interest

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in Analytical Chemistry

ChemRxiv

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