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Resolve the activation free energy into enthalpy and entropy in the Eyring equation:Taking logarithms of numerical values in fixed, consistent units givesThus for slope $s$ and intercept $b$,The logarithms imply reference units, as made explicit in the supplied numerical plot. Approximate linearity requires the activation parameters and transmission coefficient to vary little over the temperature interval; a significant activation heat-capacity difference produces curvature.

In transition state theory, $K^{‡}$ is the dimensionless equilibrium-like constant for forming the activated complex from the reactants under the chosen standard-state convention. It is not the equilibrium constant for forming the stable product.

${\Delta }_{\mathrm{r}}{G}^{\circ ,‡}$ is the standard activation free energy, ${\Delta }_{\mathrm{r}}{H}^{\circ ,‡}$ the standard activation enthalpy, and ${\Delta }_{\mathrm{r}}{S}^{\circ ,‡}$ the standard activation entropy. Each is the activated-complex quantity minus the corresponding sum for the reactants, with the unstable reaction-coordinate motion treated by the transition-state flux construction.

$[{]}^{\circ }=c^{\circ }$ is the standard concentration, conventionally $1\mathrm{mol}\mathrm{d}{\mathrm{m}}^{-3}$ for the rate units used here. Its inverse converts the attempt frequency $k_{\mathrm{B}}T/h$ into the units of a bimolecular rate constant. The stated Eyring equation assumes unit transmission coefficient.

Use the same transition state and consistent standard states in both directions. Subtracting their definitions givessoRing-forming association normally has ${\Delta }_{\mathrm{r}}{S}^{\circ }<0$. Hence the reverse activation entropy should be more positive, or less negative, than the forward value: a single adduct approaches a bond-breaking configuration rather than two molecules losing their relative motion. Its precise value and even whether it crosses zero cannot be deduced without the reaction entropy. The reverse elementary reaction is first order, so its Eyring equation has the corresponding first-order standard-state prefactor.

At fixed temperature, differentiating the Eyring equation with a pressure-independent prefactor and fixed concentration convention givesSince $\mathrm{d}G=V\mathrm{d}p-S\mathrm{d}T$, the derivative is the difference between the activated complex's partial molar volume and the sum for the reactants:If activation volume is approximately constant over the pressure range, integration givesThus plot $\ln k_2$ against pressure: its slope is $-\Delta V^{‡\circ }/RT$. Use pressure in pascals for a volume in ${\mathrm{m}}^3\mathrm{mo}{\mathrm{l}}^{-1}$. The model neglects pressure dependence of the transmission coefficient, substantial changes in mechanism, and strong curvature from a pressure-dependent activation volume. Fixed concentration-unit conventions and compression corrections matter for non-first-order rates.^[ref]

water stabilizes the planar amide more strongly relative to the twisted rotational transition region, increasing the free-energy barrier. nitrogen lone-pair donation into the carbonyl gives the C–N bond partial double-bond character through amide resonance, represented byamide bond rotation between the two amide conformations requires loss of favourable overlap. Near a strongly twisted geometry the nitrogen lone pair is less conjugated with C=O, and the charge-separated resonance in chemistry contribution is reduced. Polar water, a hydrogen bond donor, preferentially stabilizes the planar starting structures, including their polar carbonyl/resonance distribution, compared with this less conjugated rotational region. chloroform provides less of that differential stabilization. What controls the rate is the difference between the starting minimum and the transition state, not the absolute stabilization of either one in isolation.

For a first-order interpretation of the half-lives, the characteristic rate constants areThus the interconversion is 25 times slower in water. With comparable Eyring equation prefactors at the same temperature,which is about $8.0\mathrm{kJ}\mathrm{mo}{\mathrm{l}}^{-1}$ at $298\mathrm{K}$. This temperature is illustrative because none is specified for the measurements.

The two endpoint conformations remain minima separated by a twisted barrier in each solvent. The profiles are schematic, with arbitrary absolute barriers; the half-life ratio supports the relative kinetic comparison. If the quoted half-lives describe relaxation of a reversible cis/trans mixture, $k_{\mathrm{obs}}=k_f+k_r$, so the ratio directly concerns relaxation rates. Assigning the full $RT\ln 25$ difference to one microscopic forward barrier additionally requires comparable equilibrium populations or directional-rate information.