Chemistry:Effective molarity
In chemistry, the effective molarity (denoted EM)[1] is defined as the ratio between the first-order rate constant of an intramolecular reaction and the second-order rate constant of the corresponding intermolecular reaction (kinetic effective molarity)[1][2] or the ratio between the equilibrium constant of an intramolecular reaction and the equilibrium constant of the corresponding intermolecular reaction (thermodynamic effective molarity).[1][3]
- [math]\displaystyle{ EM_{kinetic} = {k_{intramolecular} \over k_{intermolecular}} }[/math]
- [math]\displaystyle{ EM_{thermo} = {K_{intramolecular} \over K_{intermolecular}} }[/math]
EM has the dimension of concentration. High EM values always indicate greater ease of intramolecular processes over the corresponding intermolecular ones. Effective molarities can be used to get a deeper understanding of the effects of intramolecularity on reaction courses.[4] In last decades, the frequency of use of effective molarity in scientific literature has shown a marked decrease,[citation needed] because this formalism is being progressively replaced by more important physical quantities.[which?]
See also
References
- ↑ 1.0 1.1 1.2 Kirby, AJ in (1980). Advances in Physical Organic Chemistry. London: Academic Press. pp. 183–278. ISBN 9780120335176.
- ↑ Dougherty, Eric V. Anslyn ; Dennis A. (2006). Modern physical organic chemistry (Dodr. ed.). Sausalito, Calif.: University Science Books. pp. 496. ISBN 9781891389313.
- ↑ Hunter, Christopher A.; Anderson, Harry L. (28 September 2009). "What is Cooperativity?". Angewandte Chemie International Edition 48 (41): 7488–7499. doi:10.1002/anie.200902490.
- ↑ Krishnamurthy, Vijay M.; Semetey, Vincent; Bracher, Paul J.; Shen, Nan; Whitesides, George M. (1 February 2007). "Dependence of Effective Molarity on Linker Length for an Intramolecular Protein−Ligand System". Journal of the American Chemical Society 129 (5): 1312–1320. doi:10.1021/ja066780e. PMID 17263415.
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