Chemical specificity | Wikipedia audio article
Channel: wikipedia tts
Date: 2019-05-04

This is an audio version of the Wikipedia Article:
https://en.wikipedia.org/wiki/Chemical_specificity


00:01:31 1 Basis
00:01:40 1.1 Binding
00:02:15 1.2 Catalysis
00:02:44 2 Types
00:03:36 2.1 Absolute specificity
00:04:35 2.2 Group specificity
00:05:43 2.3 Bond specificity
00:06:13 2.4 Stereochemical specificity
00:07:19 3 Determination
00:07:45 3.1 Application to enzyme kinetics
00:08:06 4 Significance
00:09:01 4.1 Medical research relevance
00:09:10 5 Applications
00:10:33 6 See also
00:11:24 7 References



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SUMMARY
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Chemical specificity is the ability of a protein's binding site 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. In the context of a single enzyme and a pair of binding molecules, the two ligands can be compared as stronger or weaker ligands (for the enzyme) on the basis of their dissociation constants. (A lower value corresponds to a stronger binding.)
Specificity for a set of ligands is unrelated to the ability of an enzyme to catalyze a given reaction, with the ligand as a substrate If a given enzyme has a high chemical specificity, this means that the set of ligands to which it binds is limited, such that neither binding events nor catalysis can occur at an appreciable rate with additional molecules.
An example of a protein-ligand pair whose binding activity can be described as highly specific is the antibody-antigen system. 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.