Glycosylation constitutes one of the most common, ubiquitous and complex forms of post-translational modification. It commences with the synthesis of the protein and plays a significant role in deciding its folded state, oligomerization and thus its function. Recent studies have demonstrated that N-linked glycans help proteins to fold as the stability and folding kinetics are altered with the removal of the glycans from them. Several studies have shown that it alters not only the thermodynamic stability but also the structural features of the folded proteins modulating their interactions and functions. Their inhibition and perturbations have been implicated in diseases from diabetes to degenerative disorders. The intent of this review is to provide insight into the recent advancements in the general understanding on the aspect of glycosylation driven stability of proteins that is imperative to their function and finally their role in health and disease states.
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July 2017
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The polyamine biosynthetic enzyme arginine decarboxylase has emerged multiple times from different proteins folds by convergent evolution, and has also emerged independently, at different times, from the same protein fold by pseudoconvergent evolution. In some cases, the enzyme cofactor is an internally produced pyruvoyl group, in others it is pyridoxal 5'-phosphate. The origin of this enzyme from such diverse structural classes and with different catalytic mechanisms indicates that the emergence of polyamine biosynthesis on Earth was, and is, inevitable. For more information, please see review article, “Evolution of Biosynthetic Diversity” by Anthony J. Michael, pages 2277–2299.
Review Article|
July 03 2017
Role of glycosylation in nucleating protein folding and stability
Biochem J (2017) 474 (14): 2333–2347.
Article history
Received:
February 10 2017
Revision Received:
April 14 2017
Accepted:
April 19 2017
