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- W792275245 abstract "NMR spectroscopy is a key tool for carbohydrate research. In studies with complex oligosaccharides there are limits to the amount of relevant structural information provided by these observables due to problems of signal overlapping, strong coupling and/or the scarcity of the key NOE information. Thus, there is an increasing need for additional parameters with structural information, such as residual dipolar couplings (RDCs), paramagnetic relaxation enhancements (PREs) or pseudo contact shifts (PCSs). Carbohydrates are rather flexible molecules. Therefore, NMR observables do not always correlate with a single conformer but with an ensemble of low free-energy conformers that can be accessed by thermal fluctuations. Depending on the system under study, different NMR approaches can be followed to characterize protein–carbohydrate interactions: the standard methodologies can usually be classified as “ligand-based” or “receptor-based”. The selection of the proper methodology is usually determined by the size of the receptor, the dissociation constant of the complex (KD), the availability of the labelled protein (15N, 13C) and the access to soluble receptors at enough concentration for NMR measurements." @default.
- W792275245 created "2016-06-24" @default.
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- W792275245 creator A5054938337 @default.
- W792275245 creator A5056137452 @default.
- W792275245 creator A5063186779 @default.
- W792275245 date "2015-04-10" @default.
- W792275245 modified "2023-10-16" @default.
- W792275245 title "Carbohydrate–Protein Interactions: A 3D View by NMR" @default.
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