Determination of the Rate of Monomer Interchange in a Ligand-Bound Homodimeric Protein from NOESY Cross Peaks: Application to the HIV Protease/KNI-529 Complex
- 1 March 1999
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 121 (11) , 2607-2608
- https://doi.org/10.1021/ja984041v
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- Flexibility and Function in HIV Protease: Dynamics of the HIV-1 Protease Bound to the Asymmetric Inhibitor Kynostatin 272 (KNI-272)Journal of the American Chemical Society, 1998
- Three‐dimensional solution structure of the HIV‐1 protease complexed with DMP323, a novel cyclic urea‐type inhibitor, determined by nuclear magnetic resonance spectroscopyProtein Science, 1996
- Structure of HIV-1 protease with KNI-272, a tight-binding transition-state analog containing allophenylnorstatineStructure, 1995
- Protease uninhibitedNature, 1995
- A heteronuclear correlation experiment for simultaneous determination of 15N longitudinal decay and chemical exchange rates of systems in slow equilibriumJournal of Biomolecular NMR, 1994
- Regulation of MHC Class I Transport by the Molecular Chaperone, Calnexin (p88, IP90)Science, 1994
- STRUCTURE-BASED INHIBITORS OF HIV-1 PROTEASEAnnual Review of Biochemistry, 1993
- Disulfide bond isomerization in BPTI and BPTI(G36S): An NMR study of correlated mobility in proteinsBiochemistry, 1993
- Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A.Proceedings of the National Academy of Sciences, 1988