Glycosylation is a common covalent modification on more than half of all proteins. Glycosylation occurs in many different combinations of sugars and linkages, greatly enhancing the diversity of protein chemistries, structures, and functions. In general, glycoproteins must be properly glycosylated to achieve their full bioactivity; altered glycosylation is linked to the pathophysiology of diseases ranging from cancer to rheumatoid arthritis. Currently, the impact of glycosylation on protein structure is not fully understood and difficult to predict. Although specific protein-sugar interactions are believed to contribute to structural stability, very few universal interaction patterns have been identified. Computational methods allow efficient examination of sequences with various combinations of different protein-glycan interactions. Since the Protein Data Bank contains over 3,400 glycoprotein structures, structural bioinformatics offers an effective method to sytematically discern naturally occurring, high frequency patterns of protein-sugar interactions associated with a type of protein structure. Analysis of protein-sugar interactions and the sugar orientation relative to the protein secondary structure has led to principles useful to design ultra-stable glycopeptides with, for instance, α-helix and β-turn secondary structures.

Using structural bioinformatics to design glycopeptides with enhanced secondary structure

250th National Meeting (2015)

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