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Institute for Biophysical Dynamics, Department of Chemistry, Department of Biochemistry and Molecular Biology, The University of Chicago, 929 East 57th Street, Chicago, USA
; Tel: +1-773-702-4912
Org. Biomol. Chem., 2012,10, 5887-5891
16 Mar 2012,
02 May 2012
First published online
01 Jun 2012
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.
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Organic & Biomolecular Chemistry
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