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Express each concentration value as the ratio c/c 0, where c 0 is the concentration in a [hypothetical] standard state, with a numerical value of 1, by definition. [19] Express the concentrations on the mole fraction scale. Since mole fraction has no dimension, the quotient of concentrations will, by definition, be a pure number.
An often considered quantity is the dissociation constant K d ≡ 1 / K a , which has the unit of concentration, despite the fact that strictly speaking, all association constants are unitless values. The inclusion of units arises from the simplification that such constants are calculated solely from concentrations, which is not the case.
The solvent (e.g. water) is omitted from this expression when its concentration is effectively unchanged by the process of acid dissociation. The strength of a weak acid can be quantified in terms of a dissociation constant , K a {\displaystyle K_{a}} , defined as follows, where [ H ] {\displaystyle {\ce {[H]}}} signifies the concentration of a ...
the concentration of water may be taken as being constant and the formation of the hydronium ion is implicit. AH ⇌ A − + H + Water concentration is omitted from expressions defining equilibrium constants, except when solutions are very concentrated. = [] [] [] (K defined as a dissociation constant)
The dissociation constant for a particular ligand–protein interaction can change with solution conditions (e.g., temperature, pH and salt concentration). The effect of different solution conditions is to effectively modify the strength of any intermolecular interactions holding a particular ligand–protein complex together.
depending on whether the electrode is calibrated in millivolts or pH. For convenience the concentration, [H +], is used in place of activity. In a titration of strong acid with strong alkali, the analytical concentration of the hydrogen ion is obtained from the initial concentration of acid, C i and the amount of alkali added during titration.
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K a /K s analysis will not detect such change. It will only calculate selective pressure within protein coding regions. In addition, selection that does not cause differences at an amino acid level—for instance, balancing selection—cannot be detected by these techniques. [1]