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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).
Dissociation in chemistry is a general process in which molecules (or ionic compounds such as salts, or complexes) separate or split into other things such as atoms, ...
In the simplest case it is the degree of dissociation of the solute. Then, φ is between 0 and 1 where 1 indicates 100% dissociation. However, φ can also be larger than 1 (e.g. for sucrose). For salts, electrostatic effects cause φ to be smaller than 1 even if 100% dissociation occurs (see Debye–Hückel equation);
Example Bjerrum plot: Change in carbonate system of seawater from ocean acidification.. A Bjerrum plot (named after Niels Bjerrum), sometimes also known as a Sillén diagram (after Lars Gunnar Sillén), or a Hägg diagram (after Gunnar Hägg) [1] is a graph of the concentrations of the different species of a polyprotic acid in a solution, as a function of pH, [2] when the solution is at ...
The term bond-dissociation energy is similar to the related notion of bond-dissociation enthalpy (or bond enthalpy), which is sometimes used interchangeably.However, some authors make the distinction that the bond-dissociation energy (D 0) refers to the enthalpy change at 0 K, while the term bond-dissociation enthalpy is used for the enthalpy change at 298 K (unambiguously denoted DH° 298).
Stepwise dissociation constants are each defined for the loss of a single proton. The constant for dissociation of the first proton may be denoted as K a1 and the constants for dissociation of successive protons as K a2, etc. Phosphoric acid, H 3 PO 4, is an example of a polyprotic acid as it can lose three protons.
Biotin and avidin bind with a dissociation constant of roughly 10 −15 M = 1 fM = 0.000001 nM. [7] Ribonuclease inhibitor proteins may also bind to ribonuclease with a similar 10 −15 M affinity. [8] The dissociation constant for a particular ligand–protein interaction can change with solution conditions (e.g., temperature, pH and
Because enzymes typically increase the non-catalyzed reaction rate by factors of 10 6-10 26, and Michaelis complexes [clarification needed] often have dissociation constants in the range of 10 −3-10 −6 M, it is proposed that transition state complexes are bound with dissociation constants in the range of 10 −14 -10 −23 M. As substrate ...