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The carbohydrate chains displayed on proteins and lipids mediate a broad range of physiological and pathophysiological events on cell surfaces as well as inside cells. It is estimated that at least 80% of all proteins are glycoproteins. Glycosylation affects not only the physical but also the biological properties of proteins, e.g. functional protein–protein interactions or signaling. At present, the enormous complexity of glycosylation patterns precludes simple concepts that would explain the functional role of glycosylation. One of the largest challenges in this respect is the analysis of glycosylation patterns, which cannot be deduced directly from the genome. Glycosylation is orchestrated by a huge number of highly specific glycosyltransferases, and, therefore, glycan chains must be considered as secondary gene products. As a prominent example, glycosylation of humanized antibodies used in cancer therapy is of critical importance. Wrong glycosylation patterns may cause adverse immune reactions, and eventually anaphylactic shock. Therefore, the precise analysis of glycosylation patterns of humanized monoclonal antibodies used in therapy is of utmost importance. However, the complexity and heterogeneity of dynamic glycan structures often discouraged researchers from actively challenging and addressing this important issue. Recent advances in carbohydrate NMR spectroscopy alongside with rapid glyco-technological progress have delivered a fresh perspective on the potential of NMR for the analysis of glycan structures, glycan dynamics and glycan–protein interactions. Therefore, this volume should be timely and useful not only for NMR specialists but also for a broader scientific community ranging from the general field of structural biology to biochemistry and biophysics, to molecular and cellular biology, to materials science. Finally, NMR studies on glycans will have a significant impact on the development of vaccines, adjuvants, therapeutics, biomarkers and on biomass regeneration. In view of this situation, we have collected the most up-to-date NMR applications from well-known specialists in the fields of carbohydrate NMR spectroscopy.

Finally, we would like to thank Professor Masatsune Kainosho for inviting us to edit this book as part of the New Developments in NMR series. We also thank Dr Harriet Manning of Royal Society of Chemistry for her encouragement and assistance in putting the book together.

Thomas Peters

Koichi Kato

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