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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.
Kd is the equilibrium constant for dissociation. is defined so that () ... [citation needed] and are also used in other areas of biochemistry.
Unless the complex is very long lived under gel conditions, or dissociation during electrophoresis is taken into account, the number derived is an apparent Kd. If the protein concentration is not known but the complex stoichiometry is, the protein concentration can be determined by increasing the concentration of DNA probe until further ...
The distribution constant (or partition ratio) (K D) is the equilibrium constant for the distribution of an analyte in two immiscible solvents. [1] [2] [3]In chromatography, for a particular solvent, it is equal to the ratio of its molar concentration in the stationary phase to its molar concentration in the mobile phase, also approximating the ratio of the solubility of the solvent in each phase.
The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, [1] and is the inverse of the dissociation constant. [2] It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as:
Many applications exist in biochemistry; for example, the pK a values of proteins and amino acid side chains are of major importance for the activity of enzymes and the stability of proteins. [67] Protein pK a values cannot always be measured directly, but may be calculated using theoretical methods.
KD: "I'm glad he won't … I don't want him to have to feel like he's pressured in this bubble to do what I did. I don't want any pressure for anybody that's coming into my world to do what I like ...
The dissociation rate in chemistry, biochemistry, and pharmacology is the rate or speed at which a ligand dissociates from a protein, for instance, a receptor. [1] It is an important factor in the binding affinity and intrinsic activity (efficacy) of a ligand at a receptor. [1]