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• W2052326653 abstract "Human immunodeficiency virus-1 (HIV-1) protease is catalytically active as a dimer of identical subunits that associate through noncovalent interactions. To investigate the forces stabilizing HIV-1 protease in its active form, we have studied the effects of pH and salts on structure and function of the enzyme. Enzymatic activity was measured by following the hydrolysis of a fluorogenic substrate. Dissociation of the dimer into its subunits was monitored by gel filtration, while conformational changes in the enzyme were probed by measurements of intrinsic tryptophan fluorescence. Mg 2+ ions were capable of dissociating the dimeric enzyme with a concomitant red shift and increase in quantum yield of the tryptophan fluorescence, indicating increased accessibility of tryptophan to the aqueous environment. These structural changes also were associated with a loss of catalytic activity which was insensitive to substrate concentration, consistent with noncompetitive inhibition. Both structural and functional changes could be attributed to binding of Mg 2+ ions to a site with an apparent dissociation constant of ~2 M. In contrast, increasing concentrations of Na ions up to 5 M were without effect. Increasing pH had similar effects on HIV-1 protease as increasing Mg 2+ ions concentration, with concomitant dissociation into subunits, increase in quantum yield and red shift in tryptophan fluorescence, and loss in catalytic activity. The apparent pK a for these structural and functional transitions was 6.95 ± 0.08. This value is consistent with that of an aspartic acid residue with an anomalously high pK a , which has been implicated in the catalytic activity of HIV-1 protease.Key words: human immunodeficiency virus-1 protease, dimerization, pH and salt effects." @default.
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• W2052326653 date "1994-05-01" @default.
• W2052326653 modified "2023-09-23" @default.
• W2052326653 title "Effect of pH and nonphysiological salt concentrations on human immunodeficiency virus-1 protease dimerization" @default.
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• W2052326653 doi "https://doi.org/10.1139/o94-026" @default.
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