Chemical specificity

This relationship can be described by a dissociation constant, which characterizes the balance between bound and unbound states for the protein-ligand system.

An example of a protein-ligand pair whose binding activity can be highly specific is the antibody-antigen system.

[2] Affinity maturation typically leads to highly specific interactions, whereas naive antibodies are promiscuous and bind a larger number of ligands.

[3] Conversely, an example of a protein-ligand system that can bind substrates and catalyze multiple reactions effectively is the Cytochrome P450 system, which can be considered a promiscuous enzyme due to its broad specificity for multiple ligands.

Proteases are a group of enzymes that show a broad range of cleavage specificities.

[4] The interactions between the protein and ligand substantially affect the specificity between the two entities.

A flexible protein can adapt its conformation to a larger number of ligands and thus is more promiscuous.

For example, lactase is an enzyme specific for the degradation of lactose into two sugar monosaccharides, glucose and galactose.

[10] One example is Pepsin, an enzyme that is crucial in digestion of foods ingested in our diet, that hydrolyzes peptide bonds in between hydrophobic amino acids, with recognition for aromatic side chains such as phenylalanine, tryptophan, and tyrosine.

This enzyme exhibits group specificity by allowing multiple hexoses (6 carbon sugars) as its substrate.

are the rates of the forward and backward reaction, respectively in the conversion of individual E and S to the enzyme substrate complex.

Information theory allows for a more quantitative definition of specificity by calculating the entropy in the binding spectrum.

[4] The chemical specificity of an enzyme for a particular substrate can be found using two variables that are derived from the Michaelis-Menten equation.

The higher the specificity constant of an enzyme corresponds to a high preference for that substrate.

Enzymatic specificity provides useful insight into enzyme structure, which ultimately determines and plays a role in physiological functions.

Drugs depend on the specificity of the designed molecules and formulations to inhibit particular molecular targets.

[1] Novel drug discovery progresses with experiments involving highly specific compounds.

For example, the basis that drugs must successfully be proven to accomplish is both the ability to bind the target receptor in the physiological environment with high specificity and also its ability to transduce a signal to produce a favorable biological effect against the sickness or disease that the drug is intended to negate.

Immunostaining utilizes the chemical specificity of antibodies in order to detect a protein of interest at the cellular level.

[14] Another technique that relies on chemical specificity is Western blotting, which is utilized to detect a certain protein of interest in a tissue.

This technique involves gel electrophoresis followed by transferring of the sample onto a membrane which is stained by antibodies.