Current techniques in pulse Fourier transform and rapid scan correlation 1H, 13C, 15N, and 31P nuclear magnetic resonance (NMR) spectroscopy at the highest available magnetic field strengths (200 MHz, 450 MHz, and 600 MHz) will be applied to studies of serine proteinases and glycoproteins. New methods developed in this laboratory for the study of active site residues of proteinase and proteinase inhibitors will be extended to investigation of elastase and the blood clotting proteins prothrombin, thrombin, factors IX and IXa, and factors X and Xa and their inhibitors. Comparative studies of members of the chymotrypsin family and their zymogens will be undertaken in order to learn more about the mechanism of zymogen activation, limited proteolysis, and enzymatic catalysis. It should be possible to classify the mechanism of action of proteinase inhibitors by means of NMR parameters. The experiments with glycoproteins are designed to test the usefulness of NMR spectroscopy for structural analysis of glycans and to discover if the presence of carbohydrate alters the properties of the protein or vice versa. The glycoproteins examined belong to the family of secretory inhibitors (ovomucoids) from a number of species.