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Describes the interaction of the hepatitis C virus (HCV) NS3 protease domain with its NS4A cofactor peptide at equilibrium and at pre-steady state under different physiochemical conditions. Extent of glycerol-induced stabilization varied in an HCV strain-dependent way with at least one determinant mapping to an NS3 interaction site.

Examines the complex formation between the hepatitis C virus serine protease and A synthetic NS4A cofactor peptide. Maturation cleavages that occur in the nonstructural region of the viral protein; In vitro complex formation between the NS3 protease domain.

Presents a homology model that predicts the components of the zinc binding site of the serine protease domain of NS3 protein of hepatitis C virus. Need of zinc for enzymatic activity; Properties of the metal-substituted NS3 proteinases.