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Equilibrium displacement plot

First, it is interesting to compare the equilibrium displacement plot (Fig. 10.2) with the plots of displacements from non-equilibrium stationary... [Pg.98]

Figure 13. The Gibbs energy available from a reaction, A B, depends on its displacement from equilibrium when IB)/IA) = K. The AC value is plotted against the mass-action ratio, and this is the value when B1/ A] is maintained constant in the steady state if the rate of substrate supply and substrate removal is constant. Figure 13. The Gibbs energy available from a reaction, A B, depends on its displacement from equilibrium when IB)/IA) = K. The AC value is plotted against the mass-action ratio, and this is the value when B1/ A] is maintained constant in the steady state if the rate of substrate supply and substrate removal is constant.
Provided that a value for KL is available, it is possible to use this equation to obtain a value for Kh the dissociation equilibrium constant for the inhibitor, by nonlinear least-squares analysis of the displacement curve. Alternatively, K can be calculated from the IC50, which may be obtained by simple interpolation by eye from a Hill plot or by fitting a curve to an equation of the type ... [Pg.163]

This plot represents the variation of an excessively adsorbed amount of acetonitrile with the variation of the equilibrium concentration of acetonitrile in the bulk solution. In the adsorption system the influence of adsorption forces exerted by the adsorbent surface are limited in their distance consequently, we should have limited volume where adsorbed analyte accumulates. It is also assumed that liquid is uncompressible and that molar volumes of both components do not change under the influence of adsorption forces. This leads to the displacement adsorption mechanism. [Pg.45]

Competitive inhibitors do not change the value of Vmax> which is reached when sufficiently high concentrations of the substrate are present so as to completely displace the inhibitor. However, the affinity of the substrate for the enzyme appears to be decreased in the presence of a competitive inhibitor. This happens because the free enzyme E is not only in equilibrium with the enzyme-substrate complex E. S, but also with the enzyme-inhibitor complex E. L Competitive inhibitors increase the apparent of the substrate by a factor of (1 + The evaluation of the kinetics is again greatly facilitated by the conversion of Equation 17.15 into a linear form using Line-weaver-Burk, Eadie-Hofstee, or Hanes-Woolf plots, as shown in Fig. 17.7. [Pg.729]

Figure 2.62. Potential energy plot of Mg-2H system as a function of displacement of the H atoms in two directions relative to the equilibrium position within the hydride. See text for further explanation (Sorensen, 2004f). Figure 2.62. Potential energy plot of Mg-2H system as a function of displacement of the H atoms in two directions relative to the equilibrium position within the hydride. See text for further explanation (Sorensen, 2004f).

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