DIFFERENTIAL EPITOPE MAPPING- (DEEP) STD NMR TO REVEAL THE NATURE OF PROTEIN-CARBOHYDRATE CONTACTS

摘要

Saturation Transfer Difference (STD) NMR spectroscopy is extensively used to obtain epitope maps of ligands binding to protein receptors under fast exchange conditions [1], [2]. STD NMR reveals structural details of biomolecular recognition processes, which are fundamental to direct lead optimisation efforts in drug discovery, and is an excellent technique for structural studies of protein-carbohydrate interactions.