Analysis of Glutamine Deamidation: Products, Pathways, and Kinetics

11 July 2019, Version 1
This content is a preprint and has not undergone peer review at the time of posting.

Abstract

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.

Keywords

isoaspartic acid
isoaspartate
isoglutamic acid
radical directed dissociation
epimer

Supplementary materials

Title
Description
Actions
Title
Gln SI
Description
Actions

Comments

Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.