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  2. Non-competitive inhibition - Wikipedia

    en.wikipedia.org/wiki/Non-competitive_inhibition

    When a non-competitive inhibitor is added the Vmax is changed, while the Km remains unchanged. According to the Lineweaver-Burk plot the Vmax is reduced during the addition of a non-competitive inhibitor, which is shown in the plot by a change in both the slope and y-intercept when a non-competitive inhibitor is added. [8]

  3. Fick's laws of diffusion - Wikipedia

    en.wikipedia.org/wiki/Fick's_laws_of_diffusion

    Fick's first law relates the diffusive flux to the gradient of the concentration. It postulates that the flux goes from regions of high concentration to regions of low concentration, with a magnitude that is proportional to the concentration gradient (spatial derivative), or in simplistic terms the concept that a solute will move from a region of high concentration to a region of low ...

  4. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    On the other hand, the V max will decrease relative to an uninhibited enzyme. On a Lineweaver-Burk plot, the presence of a noncompetitive inhibitor is illustrated by a change in the y-intercept, defined as 1/V max. The x-intercept, defined as −1/K M, will remain the same. In competitive inhibition, the inhibitor will bind to an enzyme at the ...

  5. Substrate inhibition in bioreactors - Wikipedia

    en.wikipedia.org/wiki/Substrate_inhibition_in...

    If the inhibitor is different from the substrate, then competitive inhibition will increase Km while Vmax remains the same, and non-competitive will decrease Vmax while Km remains the same. However, under substrate inhibiting effects where two of the same substrate molecules bind to the active sites and inhibitory sites, the reaction rate will ...

  6. Mixed inhibition - Wikipedia

    en.wikipedia.org/wiki/Mixed_inhibition

    a possible mechanism of non-competitive inhibition, a kind of mixed inhibition.. Mixed inhibition is a type of enzyme inhibition in which the inhibitor may bind to the enzyme whether or not the enzyme has already bound the substrate but has a greater affinity for one state or the other. [1]

  7. Molecular diffusion - Wikipedia

    en.wikipedia.org/wiki/Molecular_diffusion

    Molecular diffusion, often simply called diffusion, is the thermal motion of all (liquid or gas) particles at temperatures above absolute zero. The rate of this movement is a function of temperature, viscosity of the fluid and the size (mass) of the particles.

  8. Lineweaver–Burk plot - Wikipedia

    en.wikipedia.org/wiki/Lineweaver–Burk_plot

    With pure noncompetitive inhibition the apparent value of is decreased. This can be seen on the Lineweaver–Burk plot as an increased ordinate intercept with no effect on the abscissa intercept /, as pure noncompetitive inhibition does not effect substrate affinity.

  9. Diffusion - Wikipedia

    en.wikipedia.org/wiki/Diffusion

    In the phenomenological approach, diffusion is the movement of a substance from a region of high concentration to a region of low concentration without bulk motion. According to Fick's laws, the diffusion flux is proportional to the negative gradient of concentrations. It goes from regions of higher concentration to regions of lower concentration.