Tetrameric

Tetrameric refers to a molecular assembly composed of four subunits. In biochemistry and structural biology, tetramers are a common form of protein quaternary structure. Subunits can be identical, forming a homotetramer, or different, forming a heterotetramer. The four subunits come together through interfaces that are typically stabilized by noncovalent interactions, though some tetramers may involve covalent bonds or metal coordination. The overall architecture can exhibit fourfold symmetry (C4) or other symmetry arrangements such as dihedral (D2).

Tetramerization can influence function in several ways. It often enables cooperative binding or allosteric regulation, where binding at one subunit affects activity at others. It can increase structural stability, allow diverse catalytic or binding sites, and enable coordinated control of activity in response to cellular signals. The quaternary structure also permits modular evolution, as subunits can duplicate or diversify while preserving overall assembly.

In nature, many proteins assemble as tetramers. Hemoglobin is a classic example, a heterotetramer composed of two alpha and two beta subunits that enables cooperative oxygen binding. Lactate dehydrogenase can form tetrameric isozymes with different subunit compositions. Beyond biology, tetrameric arrangements occur in inorganic and supramolecular chemistry, where four-unit assemblies are designed for catalysis, signaling, or materials applications.

Techniques such as X-ray crystallography and cryo-electron microscopy are used to determine tetramer structures and interfaces, helping to elucidate how subunit organization relates to function.