Abstract

Recent advances in the conformational analysis of oligosaccharides have focused on protein-bound oligosaccharides, glycopeptides, and glycoproteins, as well as on the conformational dynamics about glycosidic linkages. Significant progress has been made possible by dramatic improvements in NMR techniques and advances in computational chemistry and technology. Transferred nuclear Overhauser effects have been used to infer the conformations of carbohydrate ligands bound to protein receptors such as antibodies, lectins and enzymes. The increased use of combined NMR spectroscopic and computational protocols has resulted in insights into the dynamics of glycan chains.

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