Search results
Results from the WOW.Com Content Network
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.
Substrate dissociation rate contributes to how large or small the enzyme velocity will be. [2] In the Michaelis-Menten model, the enzyme binds to the substrate yielding an enzyme substrate complex, which can either go backwards by dissociating or go forward by forming a product. [2] The dissociation rate constant is defined using K off. [2]
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, ions, or radicals, usually in a reversible manner.
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.
Stability constants defined in this way, are association constants. This can lead to some confusion as pK a values are dissociation constants. In general purpose computer programs it is customary to define all constants as association constants. The relationship between the two types of constant is given in association and dissociation constants.
In these applications, terms such as stability constant, formation constant, binding constant, affinity constant, association constant and dissociation constant are used. In biochemistry, it is common to give units for binding constants, which serve to define the concentration units used when the constant's value was determined.
Among the tightest known protein–protein complexes is that between the enzyme angiogenin and ribonuclease inhibitor; the dissociation constant for the human proteins is 5x10 −16 mol/L. [3] [4] Another biological example is the binding protein streptavidin, which has extraordinarily high affinity for biotin (vitamin B7/H, dissociation ...
The constants listed here are known values of physical constants expressed in SI units; that is, physical quantities that are generally believed to be universal in nature and thus are independent of the unit system in which they are measured. Many of these are redundant, in the sense that they obey a known relationship with other physical ...