Although glycation in antibodies is often dispersed throughout a large number of lysines, some studies have identified regions known as “glycation hotspots,” suggesting that specific structural characteristics control the rate of glycation. Using structural and mutational data, it was postulated that a nearby acidic residue, functioning catalytically, contributed to the conversion of the original glucose adduct, a Schiff base, into a more stable Amadori product, in addition to solvent accessibility. Thus, in order to predict glycation hotspots, we can use a structural model to look for exposed lysine residues near appropriate acidic residues.
For more: lysine glycation site analysis