4.7 Review

Common Post-translational Modifications (PTMs) of Proteins: Analysis by Up-to-Date Analytical Techniques with an Emphasis on Barley

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 71, Issue 41, Pages 14825-14837

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.3c00886

Keywords

barley; post-translationalmodification; protein; mass spectrometry

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Post-translational modifications (PTMs) play a crucial role in understanding the biological complexity generated by a small number of genes. The PTMs of barley proteins, including phosphorylation, glycation, and glycosylation, are important for metabolism and regulation. Innovative analytical approaches are needed to study and characterize PTMs in more detail.
Post-translational modifications (PTMs) of biomacromolecules can be useful for understanding the processes by which a relatively small number of individual genes in a particular genome can generate enormous biological complexity in different organisms. The proteomes of barley and the brewing process were investigated by different techniques. However, their diverse and complex PTMs remain understudied. As standard analytical approaches have limitations, innovative analytical approaches need to be developed and applied in PTM studies. To make further progress in this field, it is necessary to specify the sites of modification, as well as to characterize individual isoforms with increased selectivity and sensitivity. This review summarizes advances in the PTM analysis of barley proteins, particularly those involving mass spectrometric detection. Our focus is on monitoring phosphorylation, glycation, and glycosylation, which critically influence functional behavior in metabolism and regulation in organisms.

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