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Role of glycosylation in nucleating protein folding and stability

Jayaprakash, Nisha Grandhi and Surolia, Avadhesha (2017) Role of glycosylation in nucleating protein folding and stability. In: BIOCHEMICAL JOURNAL, 474 (14). pp. 2333-2347.

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Official URL: http://doi.org/10.1042/BCJ20170111


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.

Item Type: Journal Article
Additional Information: Copy right for this article belongs to the PORTLAND PRESS LTD, CHARLES DARWIN HOUSE, 12 ROGER STREET, LONDON WC1N 2JU, ENGLAND
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Date Deposited: 24 Aug 2017 06:25
Last Modified: 24 Aug 2017 06:25
URI: http://eprints.iisc.ac.in/id/eprint/57671

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