Proteins can be engineered with improved or novel functions by altering primary sequence. Covalent modifications offer an additional tool for protein design since they enhance the diversity of protein structure and function given by the 20 amino acids. Glycosylation is a common covalent modification that occurs on more than half of all polypeptides. Glycans function as recognition sites, mediate immune responses to pathogens, and regulate protein folding and turnover. N-linked glycosylation to asparagine occurs co-translationally in the endoplasmic reticulum potentially facilitating proper protein folding and stabilization of secondary structure. It has been suggested that specific interactions between the sugars and amino acids contribute to structural stabilization. This study characterizes protein-glycan interactions that enhance protein secondary structure. A bioinformatics analysis of the Protein Data Bank identified amino acids with the potential to stabilize specific secondary structures through such interactions. Computational methods were used to further analyze the effects of the identified constructs on secondary structures at the molecular level.

Role of glycosylation in protein structure: A bioinformatics-based computational study

249th National Meeting (2015)

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