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Molecular binding is an attractive interaction between two molecules that results in a stable association in which the molecules are in close proximity to each other. It is formed when atoms or molecules bind together by sharing of electrons.
In contrast to the definition of ligand in metalorganic and inorganic chemistry, in biochemistry it is ambiguous whether the ligand generally binds at a metal site, as is the case in hemoglobin. In general, the interpretation of ligand is contextual with regards to what sort of binding has been observed.
Wedges are used to show this, and there are two types: dashed and filled. A filled wedge indicates that the atom is in the front of the molecule; it is pointing above the plane of the paper towards the front. A dashed wedge indicates that the atom is behind the molecule; it is pointing below the plane of the paper.
The bond order of the metal ligand bond can be in part distinguished through the metal ligand bond angle (M−X−R). This bond angle is often referred to as being linear or bent with further discussion concerning the degree to which the angle is bent. For example, an imido ligand in the ionic form has three lone pairs.
A chemical bond is the association of atoms or ions to form molecules, crystals, and other structures. The bond may result from the electrostatic force between oppositely charged ions as in ionic bonds or through the sharing of electrons as in covalent bonds, or some combination of these effects.
Finally, a phosphodiester bond between the two DNA ends is formed via the nucleophilic attack of the 3'-hydroxyl at the end of a DNA strand on the activated 5′-phosphoryl group of another. [4] A nick in the DNA (i.e. a break in one strand of a double-stranded DNA) can be repaired very efficiently by the ligase. However, a complicating feature ...
The first description of cooperative binding to a multi-site protein was developed by A.V. Hill. [4] Drawing on observations of oxygen binding to hemoglobin and the idea that cooperativity arose from the aggregation of hemoglobin molecules, each one binding one oxygen molecule, Hill suggested a phenomenological equation that has since been named after him:
The "chemical ligation" concept was introduced by Kent in the early 1990s. [1] It consisted of a novel approach to the covalent condensation of unprotected peptide segments by means of "unique, mutually reactive functionalities, one on each reacting peptide segment, designed to react only with each other and not with any of the functional groups found in (native) peptides".