@book{549de0ab63ae4a3b8e9508fcfa2e1046,
title = "Probing carbohydrate-protein interactions by high- resolution NMR spectroscopy",
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.",
keywords = "Resonance Assignment, Glycosidic Linkage, Nuclear Overhauser Effect, Carbohydrate Ligand, Adjacent Monomer",
author = "S.W. Homans and R.A. Field and M.J. Milton and M. Probert and J.M. Richardson",
year = "1998",
language = "Undefined",
series = "Advances in Experimental Medicine and Biology",
}