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Dissociation constant. In chemistry, biochemistry, and pharmacology, a dissociation constant ( KD) 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 ...
e. In chemistry, an acid dissociation constant (also known as acidity constant, or acid-ionization constant; denoted ) is a quantitative measure of the strength of an acid in solution. It is the equilibrium constant for a chemical reaction. known as dissociation in the context of acid–base reactions.
The Henderson–Hasselbalch equation relates the pH of a solution containing a mixture of the two components to the acid dissociation constant, Ka of the acid, and the concentrations of the species in solution. [2] Simulated titration of an acidified solution of a weak acid ( pKa = 4.7) with alkali. To derive the equation a number of ...
Protein p. K. a. calculations. In computational biology, protein pKa calculations are used to estimate the p Ka values of amino acids as they exist within proteins. These calculations complement the p Ka values reported for amino acids in their free state, and are used frequently within the fields of molecular modeling, structural ...
An acid–base titration is a method of quantitative analysis for determining the concentration of Brønsted-Lowry acid or base (titrate) by neutralizing it using a solution of known concentration (titrant). [1] A pH indicator is used to monitor the progress of the acid–base reaction and a titration curve can be constructed.
The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, and is the inverse of the dissociation constant. It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: R + L ⇌ RL. The reaction is characterized by the on-rate ...
Titration curve. A typical titration curve of a diprotic acid, oxalic acid, titrated with a strong base, sodium hydroxide. Both equivalence points are visible. Titrations are often recorded on graphs called titration curves, which generally contain the volume of the titrant as the independent variable and the pH of the solution as the dependent ...
The substrate concentration midway between these two limiting cases is denoted by K M. Thus, K M is the substrate concentration at which the reaction velocity is half of the maximum velocity. The two important properties of enzyme kinetics are how easily the enzyme can be saturated with a substrate, and the maximum rate it can achieve.