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The structural and functional role of conserved residue G86 in HIV‐1 protease (PR) was investigated by NMR and crystallographic analyses of substitution mutations of glycine to alanine and serine (PRG86A and PRG86S). While PRG86S had undetectable catalytic activity, PRG86A exhibited ∼6000‐fold lower catalytic activity than PR. 1H‐15N NMR correlation spectra revealed that PRG86A and PRG86S are dimeric,...
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