| Range |
Figure - link kJ/mol
|
| Organism |
Generic |
| Reference |
Klebe G. Applying thermodynamic profiling in lead finding and optimization. Nat Rev Drug Discov. 2015 Feb14(2):95-110. doi: 10.1038/nrd4486. p.98 figure 1PubMed ID25614222
|
| Primary Source |
Olsson, T. S. G., Williams M. A., Pitt W. R. & Ladbury J. E. The thermodynamics of protein-ligand interactions and solvation: insights for ligand design. J. Mol. Biol. 384, 1002–1017 (2008). doi: 10.1016/j.jmb.2008.09.073.PubMed ID18930735
|
| Comments |
"The diagram is split by the thick dashed diagonal line (main diagonal) into areas where enthalpy (?H green) or entropy (-T?S red) dominate the Gibbs free energy of binding (?G). The scatter in ?G, from about -15 kJ per mol to the more favourable -60 kJ per mol, corresponds to the range that is accessible to medicinal chemistry. The perpendicular scatter shows enthalpy and entropy with opposing contributions to ?G. It spreads across a very large range, thus depicting the inherent enthalpy–entropy compensation. Data are classified according to whether they originate from medicinal chemistry optimization (blue triangles) or as biomolecules from natural sources (brown circles). The optimization that results from medicinal chemistry programmes (large bold arrow) improves ?G typically via entropically driven means." See note beneath table |
| Entered by |
Uri M |
| ID |
111405 |