Interflap Distances in HIV-1 Protease Determined by Pulsed EPR Measurements
- 17 August 2007
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 129 (36) , 11004-11005
- https://doi.org/10.1021/ja073684k
Abstract
No abstract availableKeywords
This publication has 16 references indexed in Scilit:
- Recent advances and applications of site-directed spin labelingCurrent Opinion in Structural Biology, 2006
- DeerAnalysis2006—a comprehensive software package for analyzing pulsed ELDOR dataApplied Magnetic Resonance, 2006
- The determination of pair distance distributions by pulsed ESR using Tikhonov regularizationJournal of Magnetic Resonance, 2004
- Multidrug Resistance to HIV-1 Protease Inhibition Requires Cooperative Coupling between Distal MutationsBiochemistry, 2003
- A solution NMR study of the binding kinetics and the internal dynamics of an HIV‐1 protease‐substrate complexProtein Science, 2003
- Dead-Time Free Measurement of Dipole–Dipole Interactions between Electron SpinsJournal of Magnetic Resonance, 2000
- Thermodynamic dissection of the binding energetics of KNI‐272, a potent HIV‐1 protease inhibitorProtein Science, 2000
- Sequence requirements of the HIV-1 protease flap region determined by saturation mutagenesis and kinetic analysis of flap mutantsProceedings of the National Academy of Sciences, 1997
- 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
- VMD: Visual molecular dynamicsJournal of Molecular Graphics, 1996