@inbook{cf9374547522445d8f1ee53ab8e1ec00,
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 = "Homans, {S W} and Field, {R A} and Milton, {M J} and M Probert and Richardson, {J M}",
year = "1998",
doi = "10.1007/978-1-4615-5383-0_3",
language = "English",
isbn = "978-1-4613-7457-25383-0_3",
volume = "435",
series = "Advances in Experimental Medicine and Biology",
publisher = "Springer New York",
pages = "29--38",
booktitle = "Glycoimmunology 2",
}