Glycoprotein Analysis: Using Nuclear Magnetic Resonance
Published Online: 15 SEP 2012
Copyright © 2000 John Wiley & Sons, Ltd. All rights reserved.
Encyclopedia of Analytical Chemistry
How to Cite
Leeflang, B. R. and Vliegenthart, J. F. G. 2012. Glycoprotein Analysis: Using Nuclear Magnetic Resonance . Encyclopedia of Analytical Chemistry. .
- Published Online: 15 SEP 2012
The majority of proteins are decorated with one or more covalently linked carbohydrate chains and are thus glycoproteins. These carbohydrate chains may consist of mono-, oligo-, or polysaccharides, which can affect the physiological behavior and biological functioning of the glycoprotein. Insight into the structural aspects and characteristics of glycoprotein glycosylation is an important step in unraveling the function of carbohydrate chains in a glycoprotein. In most cases, the glycan and protein moieties are cleaved and analyzed separately. Nuclear magnetic resonance (NMR) spectroscopy is a powerful tool in this respect. A plethora of NMR techniques are available to obtain NMR parameters such as chemical shift, scalar coupling constants and relaxation and cross-relaxation properties. From these, both primary structural, three-dimensional structural and dynamical features can be determined for these molecules. In this article, several aspects of glycoprotein structural studies will be discussed, and a selection of NMR experiments, including experimental conditions, will be presented.