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Chemical specificity

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Chemical specificity is the ability of binding site of a macromolecule (such as a protein) to bind specific ligands. The fewer ligands a protein can bind, the greater its specificity. Specificity describes the strength of binding between a given protein and ligand. This relationship can be described by a dissociation constant, which characterizes the balance between bound and unbound states for the protein-ligand system.

Binding siteBinding siteIn biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. The binding partner of the macromolecule is often referred to as a ligand. Ligands may include other proteins (resulting in a protein–protein interaction), enzyme substrates, second messengers, hormones, or allosteric modulators.EnzymeEnzymeLarge biological molecule that acts as a catalystThe enzyme glucosidase converts the sugar maltose into two glucose sugars. Active site residues in red, maltose substrate in black, and NADcofactor in yellow. (PDB: 1OBB​)An enzyme is a biological macromolecule, usually a protein, that acts as a biological catalyst, accelerating chemical reactions without being consumed in the process.Dissociation constantDissociation constantIn 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 component ions. The dissociation constant is the inverse of the association constant.Ligand (biochemistry)Ligand (biochemistry)In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. The etymology stems from Latin ligare, which means 'to bind'. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein. The binding typically results in a change of conformational isomerism (conformation) of the target protein.Chemical affinityChemical affinityIn chemical physics and physical chemistry, chemical affinity is the electronic property by which dissimilar chemical species are capable of forming chemical compounds. Chemical affinity can also refer to the tendency of an atom or compound to combine by chemical reaction with atoms or compounds of unlike composition. HistoryEarly theoriesThe idea of affinity is extremely old. Many attempts have been made at identifying its origins.ProteinProteinBiomolecule consisting of chains of amino acid residuesA representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red).Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acidresidues.MacromoleculeMacromoleculeA macromolecule is a "molecule of high relative molecular mass, the structure of which essentially comprises the multiple repetition of units derived, actually or conceptually, from molecules of low relative molecular mass." Polymers, which are often used in many consumer goods, are examples of macromolecules. Common macromolecules are biopolymers (RNA and DNA, proteins, and carbohydrates), polyolefins (polyethylene) and polyamides (nylon).AntigenAntigenIn immunology, an antigen (Ag) is a molecule, or portion thereof, that can bind to a specific antibody or T-cell receptor. The presence of antigens in the body may trigger an immune response. Antigens can be proteins, peptides (amino acid chains), polysaccharides (chains of simple sugars), lipids, or nucleic acids. Antigens exist on normal cells, cancer cells, parasites, viruses, fungi, and bacteria.Cytochrome P450Cytochrome P450Cytochromes P450 (P450s or CYPs) are a superfamily of enzymes containing heme as a cofactor that mostly, but not exclusively, function as monooxygenases. However, they are not omnipresent; for example, they have not been found in Escherichia coli. In mammals, these enzymes oxidize steroids, fatty acids, xenobiotics, and participate in many biosyntheses. By hydroxylation, CYP450 enzymes convert xenobiotics into hydrophilic derivatives, which are more readily excreted.AntibodyAntibodyAn antibody (Ab), or immunoglobulin (Ig), is a large protein belonging to the immunoglobulin superfamily which is used by the immune system to identify and neutralize antigens such as those that exist on bacteria and virus cells, including those that cause disease. Each individual antibody recognizes one or more specific antigens, and antigens (a portmanteau of "antibody generator") of virtually any size and chemical composition can be recognized.Affinity maturationIn immunology, affinity maturation is the process by which TFH cell-activated B cells produce antibodies with increased affinity for antigen during the course of an immune response. With repeated exposures to the same antigen, a host will produce antibodies of successively greater affinities. A secondary response can elicit antibodies with several fold greater affinity than in a primary response.CatalysisCatalysisCatalysis (, ) is the increase in rate of a chemical reaction due to an added substance known as a catalyst ( ). Catalysts are not consumed by the reaction and remain unchanged after the reaction. If the reaction is rapid and the catalyst is recycled quickly, a very small amount of catalyst often suffices; mixing, surface area, and temperature are important factors in reaction rate.

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