The interaction of glycans with other biomolecules determines the fate of various molecular signalling process and immune response pathways. The hydrogen bonding network formed by hydroxyl protons in glycans could be acting as recognition motif for its binding partners. Hence, measurement of hydroxyl exchange rates can provide insights about structural characteristics in glycans including the presence of hydrogen bonds. However, the determination of hydroxyl exchange rates using 1H-based NMR methods in protic solvents is difficult due to the fast exchange of hydroxyl proton with the solvent. In addition, interference of multiple magnetisation transfer pathways in the proton pool makes the measurements unreliable. In this presentation, I will present a novel strategy to measure isothermal hydroxyl exchange rates in glycans using chemical exchange saturation transfer (CEST) and Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion methods on 13C exploiting its two-bond deuterium isotope shift in a H2O/D2O solvent. We have measured hydroxyl exchange rates in sucrose, maltose and cellobiose at 278 K using our strategy. Our results suggest that hydroxyl exchange rates depend on several factors, including steric accessibility of hydroxyl groups. We are able to establish a distinction in hydroxyl exchange rates of hydroxyls involved in hydrogen bonding from others. Subsequently, we have used this method of hydroxyl exchange rate measurement to understand the hydrogen bonding network in terminal residues of glycans attached to red blood cell surface proteins and lipids which are responsible for blood group-specific immune responses.