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Temperature Effects on Binding Equilibrium and Reaction Rate

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Abstract

This type of investigation is quite important for the characterisation of an enzyme:

$$\Delta {G'}^{0} = -R {_\ast} T {_\ast}\ln (1/{K}_{\mathrm{ d}})\qquad \mathrm{at}\,\,25\mathrm{\!\circ \mathrm{C}}$$
(44.1)
$$\ln ({K}_{\mathrm{d}}) = -\dfrac{\Delta {H'}^{0}} {R} {_\ast} \dfrac{1} {T} + A$$
(44.2)
$$\Delta {S'}^{0} = \dfrac{\Delta {H'}^{0} - \Delta {G'}^{0}} {T}$$
(44.3)

Such experiments can be performed on a Forbes-bar (see Fig. 44.1), that allows measurements at different temperatures in parallel. The standard Gibbs free energy of ligand binding1 Δ G 0 can be determined from the dissociation constant at standard temperature (25∘C)

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Notes

  1. 1.

    Thermodynamic parameters like Δ G, ΔH or Δ S may be given for a particular set of conditions, but often more useful are data for standard conditions (25∘C, 101325Pa, pH 0, all reactants at 1M concentration. In this case, the superscript 0 is added to the abbreviation. Biologists use pH 7 instead of 0, indicated by a prime (’0). In the older literature you may find 0’ instead, IUPAC has changed the nomenclature a few years ago.

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Correspondence to Engelbert Buxbaum .

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© 2011 Springer Science+Business Media, LLC

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Buxbaum, E. (2011). Temperature Effects on Binding Equilibrium and Reaction Rate. In: Biophysical Chemistry of Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-7251-4_44

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