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  2. Hanes–Woolf plot - Wikipedia

    en.wikipedia.org/wiki/Hanes–Woolf_plot

    Hanes plot of a/v against a for Michaelis–Menten kinetics In biochemistry , a Hanes–Woolf plot , Hanes plot , or plot of a / v {\displaystyle a/v} against a {\displaystyle a} is a graphical representation of enzyme kinetics in which the ratio of the initial substrate concentration a {\displaystyle a} to the reaction velocity v ...

  3. Arrhenius plot - Wikipedia

    en.wikipedia.org/wiki/Arrhenius_plot

    In chemical kinetics, an Arrhenius plot displays the logarithm of a reaction rate constant, (⁡ (), ordinate axis) plotted against reciprocal of the temperature (/, abscissa). [1] Arrhenius plots are often used to analyze the effect of temperature on the rates of chemical reactions.

  4. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    , which is often written as , [5] represents the limiting rate approached by the system at saturating substrate concentration for a given enzyme concentration. The Michaelis constant K m {\displaystyle K_{\mathrm {m} }} is defined as the concentration of substrate at which the reaction rate is half of V {\displaystyle V} . [ 6 ]

  5. Lineweaver–Burk plot - Wikipedia

    en.wikipedia.org/wiki/Lineweaver–Burk_plot

    An example of a Lineweaver–Burk plot of 1/v against 1/a. ... is a function of the substrate concentration and two ... the limiting rate, and ...

  6. Log–log plot - Wikipedia

    en.wikipedia.org/wiki/Log–log_plot

    Bode plot (a graph of the frequency response of a system) is also log–log plot. In chemical kinetics, the general form of the dependence of the reaction rate on concentration takes the form of a power law (law of mass action), so a log-log plot is useful for estimating the reaction parameters from experiment.

  7. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    The substrate concentration midway between these two limiting cases is denoted by K M. Thus, K M is the substrate concentration at which the reaction velocity is half of the maximum velocity. [2] The two important properties of enzyme kinetics are how easily the enzyme can be saturated with a substrate, and the maximum rate it can achieve.

  8. Arrhenius equation - Wikipedia

    en.wikipedia.org/wiki/Arrhenius_equation

    In physical chemistry, the Arrhenius equation is a formula for the temperature dependence of reaction rates.The equation was proposed by Svante Arrhenius in 1889, based on the work of Dutch chemist Jacobus Henricus van 't Hoff who had noted in 1884 that the van 't Hoff equation for the temperature dependence of equilibrium constants suggests such a formula for the rates of both forward and ...

  9. Reaction progress kinetic analysis - Wikipedia

    en.wikipedia.org/wiki/Reaction_progress_kinetic...

    These cases may be distinguished by the position of the reaction progress curves relative to each other. Intercepting reactions lying below (slower rates at the same substrate concentration) the parent reactions on the rate vs. substrate concentration plot, are indicative of catalyst activation under reaction conditions.