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The degree of dissociation in gases is denoted by the symbol α, where α refers to the percentage of gas molecules which dissociate. Various relationships between K p and α exist depending on the stoichiometry of the equation. The example of dinitrogen tetroxide (N 2 O 4) dissociating to nitrogen dioxide (NO 2) will be taken.
With specific values for C a and K a this quadratic equation can be solved for x. Assuming [4] that pH = −log 10 [H +] the pH can be calculated as pH = −log 10 x. If the degree of dissociation is quite small, C a ≫ x and the expression simplifies to = and pH = 1 / 2 (pK a − log C a).
The dissociation involves cleaving of the molecular bonds in the adsorbate, and formation of new bonds with the substrate. Breaking the atomic bonds of the dissociating molecule requires a large amount of energy, thus dissociative adsorption is an example of chemisorption , where strong adsorbate-substrate bonds are created. [ 1 ]
In molecular spectroscopy, the Birge–Sponer method or Birge–Sponer plot is a way to calculate the dissociation energy of a molecule. This method takes its name from Raymond Thayer Birge and Hertha Sponer, the two physical chemists that developed it. A detailed example may be found here. [1]
In chemistry, biochemistry, and pharmacology, a dissociation constant (K D) is a specific type of equilibrium constant that measures the propensity of a larger object to separate (dissociate) reversibly into smaller components, as when a complex falls apart into its component molecules, or when a salt splits up into its component ions.
b c is the colligative molality, calculated by taking dissociation into account since the boiling point elevation is a colligative property, dependent on the number of particles in solution. This is most easily done by using the van 't Hoff factor i as b c = b solute · i , where b solute is the molality of the solution. [ 3 ]
The dissociation rate constant is defined using K off. [2] The Michaelis-Menten constant is denoted by K m and is represented by the equation K m = (K off + K cat)/ K on [definition needed]. The rates that the enzyme binds and dissociates from the substrate are represented by K on and K off respectively.
This is because the dissociation of strong electrolytes into ions is essentially complete below a concentration threshold value. The decrease in molar conductivity as a function of concentration is actually due to attraction between ions of opposite charge as expressed in the Debye-Hückel-Onsager equation and later revisions.