Structural Glycobiology by Stable-isotope-assisted NMR Spectroscopy

Recent advances in structural biology have made possible the high-throughput structural determination of proteins, which is reflected in the very rapid growth of Protein Data Bank content. In structural proteomics, recombinant proteins used for structural determination by NMR spectroscopy and X-ray crystallography are conventionally produced by use of bacterial expression systems or recently by cell-free protein expression systems and therefore do not possess carbohydrate moieties. However, many of the proteins in the living systems are covalently linked to carbohydrate moieties, which mediate molecular recognition involved in cell-cell communication, contribute to solubility and structural integrity of proteins, and determine the fates of glycoproteins in cells, i.e. folding, transport, and degradation via interactions with a variety of intra-cellular lectins [1,2].