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Issue 30, 2012
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Ionization state of the catalytic dyad Asp25/25′ in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis

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Abstract

Total chemical synthesis was used to site-specifically 13C-label active site Asp25 and Asp25′ residues in HIV-1 protease and in several chemically synthesized analogues of the enzyme molecule. 13C NMR measurements were consistent with a monoprotonated state for the catalytic dyad formed by the interacting Asp25, Asp25′ side chain carboxyls.

Graphical abstract: Ionization state of the catalytic dyad Asp25/25′ in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis

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Publication details

The article was received on 16 Mar 2012, accepted on 02 May 2012 and first published on 01 Jun 2012


Article type: Paper
DOI: 10.1039/C2OB25569C
Citation: Org. Biomol. Chem., 2012,10, 5887-5891
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    Ionization state of the catalytic dyad Asp25/25′ in the HIV-1 protease: NMR studies of site-specifically 13C labelled HIV-1 protease prepared by total chemical synthesis

    V. Yu. Torbeev and S. B. H. Kent, Org. Biomol. Chem., 2012, 10, 5887
    DOI: 10.1039/C2OB25569C

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