Calculating proton uptake/release and binding free energy taking into account ionization and conformation changes induced by protein-inhibitor association: Application to plasmepsin, cathepsin D and endothiapepsin-pepstatin complexes
- 2 April 2004
- journal article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 56 (3) , 572-584
- https://doi.org/10.1002/prot.20107
Abstract
No abstract availableKeywords
This publication has 60 references indexed in Scilit:
- Novel Uncomplexed and Complexed Structures of Plasmepsin II, an Aspartic Protease from Plasmodium falciparumJournal of Molecular Biology, 2003
- Computer Simulation of Protein−Protein InteractionsThe Journal of Physical Chemistry B, 2001
- Electrostatic aspects of protein–protein interactionsCurrent Opinion in Structural Biology, 2000
- Thermodynamic linkage between the binding of protons and inhibitors to HIV‐1 proteaseProtein Science, 1999
- Dissection of the pH Dependence of Inhibitor Binding Energetics for an Aspartic Protease: Direct Measurement of the Protonation States of the Catalytic Aspartic Acid Residues,Biochemistry, 1997
- Protein−Protein Interactions: Interface Structure, Binding Thermodynamics, and Mutational AnalysisChemical Reviews, 1997
- Electrostatic interactions in hirudin-thrombin bindingBiophysical Chemistry, 1996
- Principles of protein-protein interactions.Proceedings of the National Academy of Sciences, 1996
- Thermodynamic Mapping of the Inhibitor Site of the Aspartic Protease EndothiapepsinJournal of Molecular Biology, 1995
- Isothermal titration calorimetryAnalytical Chemistry, 1990