Search results
Results From The WOW.Com Content Network
Affinity (taxonomy) – mainly in life sciences or natural history – refers to resemblance suggesting a common descent, phylogenetic relationship, or type. [1] The term does, however, have broader application, such as in geology (for example, in descriptive and theoretical works [2] [3]), and similarly in astronomy (for example, see "Centaur object" in the context of 2060 Chiron's close ...
Low-affinity binding (high K i level) implies that a relatively high concentration of a ligand is required before the binding site is maximally occupied and the maximum physiological response to the ligand is achieved. In the example shown to the right, two different ligands bind to the same receptor binding site.
Avidity (functional affinity) is the accumulated strength of multiple affinities. [2] For example, IgM is said to have low affinity but high avidity because it has 10 weak binding sites for antigen as opposed to the 2 stronger binding sites of IgG, IgE and IgD with higher single binding affinities. [citation needed]
Allosteric modulators can alter the affinity and efficacy of other substances acting on a receptor. A modulator may also increase affinity and lower efficacy or vice versa. [ 4 ] Affinity is the ability of a substance to bind to a receptor .
A good fit corresponds with high affinity and low K d. The final biological response (e.g. second messenger cascade, muscle-contraction), is only achieved after a significant number of receptors are activated. Affinity is a measure of the tendency of a ligand to bind to its receptor. Efficacy is the measure of the bound ligand to activate its ...
In open nomenclature it indicates that available material or evidence suggests that the proposed species is related to, has an affinity to, but is not identical to, the species with the binomial name it comes after. [1] The Latin word affinis can be translated as "closely related to", or "akin to". [2]
Affinity chromatography is a method of separating a biomolecule from a mixture, based on a highly specific macromolecular binding interaction between the biomolecule ...
Hemoglobin's oxygen binding affinity (see oxygen–haemoglobin dissociation curve) is inversely related both to acidity and to the concentration of carbon dioxide. [1] That is, the Bohr effect refers to the shift in the oxygen dissociation curve caused by changes in the concentration of carbon dioxide or the pH of the environment.