Range |
~15 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.96 right column 2nd paragraphPubMed 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 |
"This value also sets a lower affinity limit of ~15kJ per mol for complex formation, as reflected in the thermodynamic data compiled by Olsson et al. [primary source]. These authors collected ITC [isothermal titration calorimetry] data for complexes containing ligands from natural biological sources and medicinal chemistry projects, and they plotted them on a diagram of ?H against -T?S (FIG. 1 BNID 111405)." |
Entered by |
Uri M |
ID |
111404 |