Issue 30, 2012

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

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

Supplementary files

Article information

Article type
Paper
Submitted
16 Mar 2012
Accepted
02 May 2012
First published
01 Jun 2012

Org. Biomol. Chem., 2012,10, 5887-5891

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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