Electrostatic effects play an essential role in specific molecular recognition and molecular assembly in many biologically important molecules. The specific electric field at the active site also regulates the catalytic reaction of a protein. Moreover, intramolecular or inter-subunit electrostatic interactions, such as saltbridges, hydrogen bonds, and charge-dipole interactions, are considered to work to stabilize protein molecules. Those electrostatic roles recently observed in proteins are reviewed with a description of the origins and principles of electrostatic forces, and analyses will be made using simple models to illuminate the physical basis.

Implementation and regulation of the molecular mechanisms underlying biological processes is dependent on direct interactions between biological molecules. These interactions are characterised by specific binding between at least one molecule and another, and for binding to occur the molecules must be able to come close enough to each other to make contact. One of the partners in the interaction is invariably a macromolecule (e.g. protein or DNA) or an assembly of large size, such as a lipid bilayer. The interaction may take place with the partners in solution, or with at least one attached to a biological surface (e.g. a membrane) or a very large structure such as a chromosome. Where the partners are part of a membrane or other large structure then there must be a mechanism, such as lateral diffusion in the plane of the membrane, that permits them to come together close enough for interaction.