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Journal Article

The conformational basis of asparagine-linked glycosylation

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Citation

Imperiali, B., & O'Connor, S. E. (1998). The conformational basis of asparagine-linked glycosylation. Pure and Applied Chemistry, 70(1), 33-40. doi:10.1351/pac199870010033.


Cite as: https://hdl.handle.net/21.11116/0000-0002-A18D-9
Abstract
The structural and functional integrity of many proteins is highly dependent upon enzyme catalyzed covalent modification reactions. The timing of these transformations may be co-translational, occurring as a protein is being biosynthesized or post-translational, acting on folded protein substrates. Our research focuses on understanding the conformational basis of specificity and selectivity in the process of co-translational protein glycosylation. This objective presents a significant challenge because the opportunities for competing transformations on the densely functionalized protein substrate in this reaction are innumerable. Since enzyme-catalyzed glycosylation is an essential eukaryotic process, an understanding of the origin of specificity is of utmost importance both to fundamental biochemistry and to a consideration of the mechanisms of homeostatic control.