NMR Spectroscopy and Computer Modeling of Carbohydrates Recent Advances

In the past ten years, the interest in the functional and structural aspects of carbohydrates and glycoconjugates has increased enormously. Great insights have been made into the mode of action of glycans in cells, tissues, organs and organisms. As more and more information becomes known implicating carbohydrates in biological function, increasing pressure is placed on all aspects of biophysical methods to adapt and advance in order to provide structural insight into the biology of carbohydrates and conjugated glycans. Many existing tools that have served admirably to probe structure-function relationships in proteins are difficult or impossible to apply to complex glycans and glycoproteins. Established structural methods, such as X-ray diffraction or NMR spectroscopy also face enormous challenges when applied to the study of biologically relevant glycans in glycoproteins. Because of the challenges and limitations of traditional experimental methods, computational techniques can contribute unique insight into the relationship between oligosaccharide structure and biological function. Perhaps in no other field can biomolecular calculations make as major a contribution; whether they serve to provide models to assist in the interpretation of otherwise insufficient experimental data, or to provide a priory models for the structure of oligosaccharides, or insight into the mechanisms of carbohydrate recognition. From the application of quantum mechanics in the study of carbohydrate-processing enzymes, to the classical dynamics simulation of oligosaccharides and their protein complexes, the range of systems being examined theoretically is rapidly expanding. Given the structural diversity and flexibility of carbohydrates, it is not surprising that both experimental and theoretical methods face many unique challenges. Contained within this text are examples of the latest NMR and computational methods applied to oligosaccharides and their complexes with proteins.