Kumar, A and Narayanan, V and Sekhar, A (2020) Characterizing Post-Translational Modifications and Their Effects on Protein Conformation Using NMR Spectroscopy. In: Biochemistry, 59 (1). pp. 57-73.
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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 NMR studies that have mapped the conformational changes ensuing from these PTMs as well as evaluated their relation to function. The NMR toolbox is expanding rapidly with experiments available to probe not only the average structure of biomolecules but also how this structure changes with time on time scales ranging from picoseconds to seconds. The atomic resolution insights into the biomolecular structure, dynamics, and mechanism accessible from NMR spectroscopy ensure that NMR will continue to be at the forefront of research in the structural biology of PTMs. © 2019 American Chemical Society.
| Item Type: | Journal Article |
|---|---|
| Publication: | Biochemistry |
| Publisher: | American Chemical Society |
| Additional Information: | The copyright for this article belongs to the Authors. |
| Keywords: | Acetylation; Biomolecules; Gene encoding; Nuclear magnetic resonance spectroscopy; Proteins, Atomic resolution; Average structure; Biomolecular structures; Conformational change; Eukaryotic proteins; Post-translational modifications; Protein conformation; Structural biology, Conformations, acetylation; article; conformational transition; glycosylation; nuclear magnetic resonance spectroscopy; protein conformation; protein function; protein processing; bacterium; chemistry; human; metabolism; nuclear magnetic resonance; phosphorylation; protein conformation; protein processing, glycoprotein; phosphoprotein, Acetylation; Bacteria; Glycoproteins; Glycosylation; Humans; Nuclear Magnetic Resonance, Biomolecular; Phosphoproteins; Phosphorylation; Protein Conformation; Protein Processing, Post-Translational |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 04 Jan 2023 11:50 |
| Last Modified: | 04 Jan 2023 11:50 |
| URI: | https://eprints.iisc.ac.in/id/eprint/79473 |
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