Characterizing Post-Translational Modifications and Their Effects on Protein Conformation Using NMR Spectroscopy.

ABSTRACT: The diversity of the cellular proteome substantially exceeds the number of genes coded by the DNA of an organism because one or more residues in a majority of eukaryotic proteins are post-translationally modified (PTM) by the covalent conjugation of specific chemical groups. We now know that PTMs alter protein conformation and function in ways that are not entirely understood at the molecular level. NMR spectroscopy has been particularly successful as an analytical tool in elucidating the themes underlying the structural role of PTMs. In this Perspective, we focus on the NMR-based characterization of three abundant PTMs: phosphorylation, acetylation, and glycosylation. We detail NMR methods that have found success in detecting these modifications at a site-specific level. We also highlight

SUBMITTER: Kumar A 

PROVIDER: S-EPMC7115964 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature