Dimerer

Dimerer is the plural form of dimer in several languages, used to refer to a molecule composed of two subunits bound together. A dimer consists of two monomers that can be identical (homodimer) or different (heterodimer). Dimerization can occur through covalent bonds, such as disulfide bridges, or through noncovalent interactions including hydrogen bonds, ionic contacts, and hydrophobic effects. Dimers occur in chemistry as well as biology and are often important for molecular stability, specificity, or activity.

In biology, many proteins function as dimers, and dimerization can be essential for activity, DNA binding, or signaling. Receptor proteins frequently dimerize upon ligand binding, triggering intracellular cascades. Transcription factors often form dimers to recognize specific DNA sequences. Some enzymes require dimerization to assemble functional active sites or to regulate catalytic activity. Dimers can be stable components of a complex or form transient assemblies in response to cellular conditions.

Structural interfaces between the two subunits vary and are stabilized by motifs such as coiled coils or leucine zippers, which favor homodimeric or heterodimeric associations. Mutations that disrupt dimer interfaces can alter function and contribute to disease, while engineered stabilization of dimers is a strategy in drug design and protein engineering.

Techniques to study dimers include size-exclusion chromatography, analytical ultracentrifugation, cross-linking followed by mass spectrometry, and high-resolution structural techniques such as X-ray crystallography and cryo-electron microscopy. Native mass spectrometry and small-angle scattering provide information on stoichiometry and arrangement in solution, while computational approaches can predict potential dimerization from sequence and structural data.