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  2. Henderson–Hasselbalch equation - Wikipedia

    en.wikipedia.org/wiki/Henderson–Hasselbalch...

    The Henderson–Hasselbalch equation can be used to model these equilibria. It is important to maintain this pH of 7.4 to ensure enzymes are able to work optimally. [10] Life threatening Acidosis (a low blood pH resulting in nausea, headaches, and even coma, and convulsions) is due to a lack of functioning of enzymes at a low pH. [10]

  3. Free base - Wikipedia

    en.wikipedia.org/wiki/Free_base

    However, since blood is buffered with carbonate at physiological pH (near 7.4), free-base amines will be rapidly converted back into their acid form. In fact, 94.19% of cocaine will exist as the acid form under equilibrium at pH=7.4, calculated using the Henderson–Hasselbalch equation assuming a pKa of 8.61. [1]

  4. Weak base - Wikipedia

    en.wikipedia.org/wiki/Weak_base

    With pOH obtained from the pOH formula given above, the pH of the base can then be calculated from =, where pK w = 14.00. A weak base persists in chemical equilibrium in much the same way as a weak acid does, with a base dissociation constant ( K b ) indicating the strength of the base.

  5. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...

  6. Acid dissociation constant - Wikipedia

    en.wikipedia.org/wiki/Acid_dissociation_constant

    It is very difficult to measure pH values of less than two in aqueous solution with a glass electrode, because the Nernst equation breaks down at such low pH values. To determine p K values of less than about 2 or more than about 11 spectrophotometric [ 60 ] [ 61 ] or NMR [ 62 ] [ 63 ] measurements may be used instead of, or combined with, pH ...

  7. Buffer solution - Wikipedia

    en.wikipedia.org/wiki/Buffer_solution

    Buffer capacity falls to 33% of the maximum value at pH = pK a ± 1, to 10% at pH = pK a ± 1.5 and to 1% at pH = pK a ± 2. For this reason the most useful range is approximately pK a ± 1. When choosing a buffer for use at a specific pH, it should have a pK a value as close as possible to that pH. [2]

  8. Determination of equilibrium constants - Wikipedia

    en.wikipedia.org/wiki/Determination_of...

    For example, with pH titration data, if pH is measured to 2 decimal places, the errors of log 10 β should not be much larger than 0.01. In exploratory work where the nature of the species present is not known in advance, several different chemical models may be tested and compared.

  9. Equilibrium constant - Wikipedia

    en.wikipedia.org/wiki/Equilibrium_constant

    The free energy change, dG r, can be expressed as a weighted sum of change in amount times the chemical potential, the partial molar free energy of the species. The chemical potential, μ i, of the ith species in a chemical reaction is the partial derivative of the free energy with respect to the number of moles of that species, N i