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-Reference-Cited by-同舟云学术

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

Published:2012 Issue:30 Volume:10 Page:5887
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Torbeev Vladimir Yu.,Kent Stephen B. H.

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2012/OB/C2OB25569C

Reference13 articles.

1. INHIBITORS OF HIV-1 PROTEASE: A Major Success of Structure-Assisted Drug Design

2. Structure of HIV-1 protease in complex with potent inhibitor KNI-272 determined by high-resolution X-ray and neutron crystallography

3. Crystal Growth Procedure of HIV-1 Protease-Inhibitor KNI-272 Complex for Neutron Structural Analysis at 1.9 Å Resolution

4. NMR and X-ray Evidence That the HIV Protease Catalytic Aspartyl Groups Are Protonated in the Complex Formed by the Protease and a Non-Peptide Cyclic Urea-Based Inhibitor

5. Solution NMR Evidence That the HIV-1 Protease Catalytic Aspartyl Groups Have Different Ionization States in the Complex Formed with the Asymmetric Drug KNI-272

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