THE CONFORMATIONAL BASIS OF ASPARAGINE-LINKED GLYCOSYLATION

The structural and functional integrity of many proteins is highly dep endent upon enzyme catalyzed covalent modification reactions. The timi ng of these transformations may be co-translational, occurring as a pr otein is being biosynthesized or post-translational, acting on folded protein substrates. Our research focuses on understanding the conforma tional basis of specificity and selectivity in the process of co-trans lational protein glycosylation. This objective presents a significant challenge because the opportunities for competing transformations on t he densely functionalized protein substrate in this reaction are innum erable. Since enzyme-catalyzed glycosylation is an essential eukaryoti c 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.