The purpose of this research is to discover the general features of the conformation of glycopeptides and their related oligosaccharides. We will explore the relationship between biological function and the different types of glycopeptide linkage and of oligosaccharide covalent structure. This goal will be achieved by applying nuclear magnetic resonance spectroscopy and conformational energy calculations to a few specific and well characterized model glycopeptides, glycoproteins and oligosaccharide systems which are chosen for their simplicity and availabiltiy in sufficient purity and quantity for nmr experiments. The model systems will include antifreeze glycoprotein from the blood of Antarctic fish, amino sugar containing oligosaccharides from human milk, chitin oligosaccharides and the glycopeptide of fetuin. The nmr experiments will include amide proton exchange rates measured by transfer of solvent saturation, line broadening by paramagnetic spin label and nuclear Overhauser effect. Conformational calculations in glycopeptides and oligosaccharides will utilize Monte Carlo methods to search the dihedral angles in a conformational space in which potential energies are constructed from empirical energy functions.
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