NMR analysis of carbohydrate-protein interactions.

摘要: Carbohydrate-protein interactions are frequently characterized by dissociation constants in the microM to mM range. This is normally associated with fast rates of corresponding complexes, turn leading exchange on nuclear magnetic resonance (NMR) chemical shift time scale and NMR relaxation scale. Therefore, experiments that take advantage well suited study carbohydrate-protein interactions. In general, it possible analyze ligand binding observing either protein signals or resonances. Because most receptor proteins which carbohydrates bind rather large molecular weights significantly exceeding 30 kDa, analysis spectra not trivial, only very few studies have been addressing this issue so far. We, therefore, focus employ observation free ligand, is, carbohydrate bound state. Two types extremely valuable at atomic resolution. Whereas transferred Overhauser effect (NOE) deliver bioactive conformations proteins, saturation transfer difference (STD) provide epitopes information about thermodynamics kinetics. We demonstrate power a combined NOE/STD approach for complexes using selected examples.