Homodimerisation

Homodimerisation is a biological process where two identical protein molecules or other biomolecules bind together to form a complex. This complex, consisting of two identical subunits, is called a homodimer. The interaction is specific, meaning the molecules recognize and bind to each other through non-covalent forces such as hydrogen bonds, ionic interactions, and hydrophobic effects. This binding can significantly alter the function of the individual molecules. For instance, in proteins, homodimerisation can lead to the formation of an active enzyme, a regulatory complex, or a structural component. Many cellular processes rely on homodimerisation, including signal transduction, gene regulation, and protein-protein interactions. The ability of molecules to undergo homodimerisation is often determined by specific regions within their structure, known as dimerisation domains. These domains are conserved across species for many proteins that form homodimers. The formation and dissociation of homodimers are dynamic processes that can be influenced by cellular conditions, such as pH, temperature, and the presence of other molecules. Understanding homodimerisation is crucial for comprehending the intricate mechanisms of biological systems and for developing targeted therapeutic interventions.