Entropy loss by merging two molecules
Range | -9 to -45 kJ/mol |
---|---|
Organism | Generic |
Reference | Mark S. Searle , Dudley H. Williams, The cost of conformational order: entropy changes in molecular associations. J. Am. Chem. Soc., 1992, 114 (27), pp 10690–10697 DOI: 10.1021/ja00053a002 abstract |
Comments | "When entropies of sublimation are corrected by Trouton’s rule for condensation to a liquid, [investigators] conclude that some bimolecular associations to form complexes with little exothermicity may have relatively small adverse entropies, which may lie anywhere in the range -9 to -45 kJ/mol (in terms of T?S at 300K), opposing binding by a factor of 10^-1.6 to 10^-8 M^-1. These “enthalpy/entropy compensations” are of general relevance to binding interactions of biological importance and are discussed with respect to the binding of agonists versus antagonists to a common receptor site." |
Entered by | Uri M |
ID | 111419 |