Factorising ligand affinity: a combined thermodynamic and crystallographic study of trypsin and thrombin inhibition†
- 26 October 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 313 (3) , 593-614
- https://doi.org/10.1006/jmbi.2001.5062
Abstract
No abstract availableKeywords
This publication has 61 references indexed in Scilit:
- Crystallographic and Calorimetric Analysis of Peptide Binding to OppA ProteinJournal of Molecular Biology, 1999
- Synthetic Inhibitors of Thrombin and Factor Xa: From Bench to BedsideThrombosis Research, 1999
- Relating structure to thermodynamics: The crystal structures and binding affinity of eight OppA‐peptide complexesProtein Science, 1999
- Small-molecule direct thrombin inhibitorsExpert Opinion on Therapeutic Patents, 1997
- New thrombin inhibitors in cardiovascular diseaseCurrent Opinion in Chemical Biology, 1997
- What Can We Learn from Molecular Recognition in Protein–Ligand Complexes for the Design of New Drugs?Angewandte Chemie International Edition in English, 1996
- Significant discrepancies between van't hoff and calorimetric enthalpies. IIProtein Science, 1995
- Win some, lose some: enthalpy-entropy compensation in weak intermolecular interactionsChemistry & Biology, 1995
- Significant discrepancies between van't Hoff and calorimetric enthalpies.Proceedings of the National Academy of Sciences, 1995
- Acquisition and use of calorimetric data for prediction of the thermodynamics of ligand-binding and folding reactions of proteinsCurrent Opinion in Biotechnology, 1994