Abstract
An important requirement for a detailed understanding of the molecular basis of the interaction of a carbohydrate with its protein receptor is a high-resolution three dimensional structure of the complex. Historically, such structural information has derived from crystallographic studies which can illustrate in detail the precise nature of certain carbohydrate-protein interactions in the solid state (reviewed by Cambillau (1995)). In contrast, few high-resolution structural studies of glycan-protein interactions in solution using nuclear magnetic resonance have been reported. The solution structure of the complex is of importance since a comparison with the solution structure of the free ligand may be more meaningful, and moreover the dynamics of the system are accessible from relaxation time measurements.
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Homans, S.W., Field, R.A., Milton, M.J., Probert, M., Richardson, J.M. (1998). Probing Carbohydrate-Protein Interactions by High-Resolution NMR Spectroscopy. In: Axford, J.S. (eds) Glycoimmunology 2. Advances in Experimental Medicine and Biology, vol 435. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5383-0_3
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DOI: https://doi.org/10.1007/978-1-4615-5383-0_3
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