X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies
- 28 January 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 295 (4) , 953-962
- https://doi.org/10.1006/jmbi.1999.3411
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- Prediction of binding constants of protein ligands: A fast method for the prioritization of hits obtained from de novo design or 3D database search programsJournal of Computer-Aided Molecular Design, 1998
- Current computational tools for de novo ligand designCurrent Opinion in Biotechnology, 1996
- Structure of the FKBP12-Rapamycin Complex Interacting with Binding Domain of Human FRAPScience, 1996
- Computational combinatorial chemistry for de novo ligand design: Review and assessmentPerspectives in Drug Discovery and Design, 1995
- Three‐dimensional structure and actions of immunosuppressants and their immunophilinsThe FASEB Journal, 1995
- The development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structureJournal of Computer-Aided Molecular Design, 1994
- A fast and efficient method for 2D and 3D molecular shape descriptionJournal of Computer-Aided Molecular Design, 1992
- LUDI: rule-based automatic design of new substituents for enzyme inhibitor leadsJournal of Computer-Aided Molecular Design, 1992
- The computer program LUDI: A new method for the de novo design of enzyme inhibitorsJournal of Computer-Aided Molecular Design, 1992
- Hydrogen bonding. Part 9. Solute proton donor and proton acceptor scales for use in drug designJournal of the Chemical Society, Perkin Transactions 2, 1989