Glycan microarrays are being constructed containing glycosaminoglycans having different sequences at each spatially addressable location. These glycan chains are either first, purified, structural characterized and then immobilized or are synthesized at site. By probing such glycan microarrays with proteins from a given cell, tissue or organism the interactome can be established.

The thermodynamic (∆H) and kinetic (k_on/k_off) properties of proteincarbohydrate interactions are important parameters to understand binding. The ∆H, ∆S and stoichiometry of binding can be measured using isothermal titration calorimetry (ITC) while the k_on/k_off , K_assoc, K_dissoc, K_eq can be conveniently measured using surface plasmon resonance (SPR). SPR and ITC can also provide information on conformation changes in binding, cooperativity, ionic vs.

The atomic contacts between glycosaminoglycan and its binding protein are determined by single crystal X-ray crystallography. The first high-resolution co-crystal