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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

    Arrhenius plots are often used to analyze the effect of temperature on the rates of chemical reactions. For a single rate-limited thermally activated process, an Arrhenius plot gives a straight line, from which the activation energy and the pre-exponential factor can both be determined.

  4. Reaction progress kinetic analysis - Wikipedia

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

    c) The rate of reaction progress (product formation) is monitored over time by methods such as reaction progress calorimetry or may be obtained by taking the first derivative of (a). d) Describing the rate of reaction progress with respect to consumption of starting material spreads the data into a more informative distribution than observed in ...

  5. 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 ...

  6. 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 ]

  7. Competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Competitive_inhibition

    Increasing the substrate concentration would diminish the "competition" for the substrate to properly bind to the active site and allow a reaction to occur. [3] When the substrate is of higher concentration than the concentration of the competitive inhibitor, it is more probable that the substrate will come into contact with the enzyme's active ...

  8. Sabatier principle - Wikipedia

    en.wikipedia.org/wiki/Sabatier_principle

    At high values of Δ f H, desorption becomes the rate-limiting step. The maximum rate, which is observed for the platinum group metals in this case, requires intermediate values of Δ f H, with the rate being a combination of the rate of adsorption and the rate of desorption. [3] Catalysts can exceed the Sabatier limit via catalytic resonance.

  9. Plot (graphics) - Wikipedia

    en.wikipedia.org/wiki/Plot_(graphics)

    The graphs can be used together to determine the economic equilibrium (essentially, to solve an equation). Simple graph used for reading values: the bell-shaped normal or Gaussian probability distribution, from which, for example, the probability of a man's height being in a specified range can be derived, given data for the adult male population.