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.
Total chemical synthesis was used to site-specifically (13)C-label active site Asp25 and Asp25' residues in HIV-1 protease and in several chemically synthesized analogues of the enzyme molecule. (13)C NMR measurements were consistent with a monoprotonated state for the catalytic dyad formed by the interacting Asp25, Asp25' side chain carboxyls.
Institute for Biophysical Dynamics, Department of Chemistry, The University of Chicago, 929 East 57th Street, Chicago, Illinois 60637, USA.
Vladimir Yu
VY
Torbeev
Stephen B H
SB
Kent
D001224:Aspartic Acid; D001665:Binding Sites; D055162:Biocatalysis; D002247:Carbon Isotopes; D060326:Chemistry Techniques, Synthetic; D016333:HIV Protease / Q000737:chemistry* / Q000378:metabolism*; D015497:HIV-1 / Q000201:enzymology*; D007553:Isotope Labeling; D056004:Molecular Dynamics Simulation; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D013379:Substrate Specificity
D002247:Carbon Isotopes; D001224:Aspartic Acid; D016333:HIV Protease