Abstract
Growing evidence reveals that glycans attached to proteins contribute not only to their solubility or stability but also to the tertiary structure of functional sites in proteins. It is becoming more and more important to elucidate the role of glycans from the structural aspects in the basic life science and applied science field, such as drug development. In this situation, we have been developing a methodology for analyzing the structure of glycoconjugates by nuclear magnetic resonance (NMR) spectroscopy. In particular, we have established a systematic method for stable isotope labeling of glycoproteins with a variety of techniques based on synthetic chemistry, enzyme chemistry and cell cultivating. Hence, it is possible to analyze the structure, dynamics and interaction of glycoproteins at atomic resolution.
