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Activation free energy functional sites

Figure 19. Calculated contributions to the free energy functions, for the hydride-transfer step (1 in Fig. 18.) of the lactate dehydrogenase reaction in a reference solvent cage (w, left) and in 1 he protein active site p, right). The Agf s are given as functions of the corresponding energy gaps (the Ac s) which are taken as the... Figure 19. Calculated contributions to the free energy functions, for the hydride-transfer step (1 in Fig. 18.) of the lactate dehydrogenase reaction in a reference solvent cage (w, left) and in 1 he protein active site p, right). The Agf s are given as functions of the corresponding energy gaps (the Ac s) which are taken as the...
Fig. 16. A. Plot of log iNa as a function of T 1 (°K) using the experimental values of the rate constants and the location of the binding sites in Eq. 4. The Gibbs free energy of activation is calculated from Eq. 3 the AS are taken to be zero, and the current is calculated by means of Eq. 4. The purpose is to demonstrate that multibarrier channel transport can be seen as single rate process with average values for the enthalpies of activation. Non-linearity of such a plot is then taken to arise form the dynamic nature of the channel. Fig. 16. A. Plot of log iNa as a function of T 1 (°K) using the experimental values of the rate constants and the location of the binding sites in Eq. 4. The Gibbs free energy of activation is calculated from Eq. 3 the AS are taken to be zero, and the current is calculated by means of Eq. 4. The purpose is to demonstrate that multibarrier channel transport can be seen as single rate process with average values for the enthalpies of activation. Non-linearity of such a plot is then taken to arise form the dynamic nature of the channel.

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Activating function

Activation free energy

Activation function

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Free energy functional

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Free functional

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