Verevka S. Structural backgrounds of inter-molecular recognition and complex-formation of serine proteinases

Serine proteinases and physiological and pathological processes. Determination of localization, ligands specificity and functional role of uncatalytic areas of intermolecular co-operation of serine proteinases of chymotrypsin-trypsin type and their role in adjusting of interprotein recognition and complex-forming. Chemical synthesis, affinity chromatography, enzymatic kinetics. The group of affinity sorbents for purification of chymotrypsin-trypsin-like proteinases has been created and tested. The dependence of their affinity properties from immobilized ligands structure has been shown. The localization and functional roles of the allosteric site of serine proteinases have been identified. Principle new polymer inhibitor of serine proteinases has been synthesized. Estimated principles of inter-protein recognition and complex-forming allowed to explain the main anomalies of prion-mediated pathologies as well as to ground their place in the line of folding diseases. Methodical approaches for detection ofprion pathogen iso-form and its elimination from the protein mixtures were proposed. Sphere of the use - bioorganic chemistry, biochemistry and medicine.