High Quality Content by WIKIPEDIA articles! A tetramer is a protein with four subunits (tetrameric). There are homo-tetramers (all subunits are identical) such as glutathione S-transferase or single-strand binding protein, dimers of hetero-dimers such as hemoglobin (a dimer of an alpha/beta dimer), and hetero-tetramers, where each subunit is different. The interactions between subunits forming a tetramer is primarily determined by non covalent interaction. Hydrophobic effects, hydrogen bonds and electrostatic interactions are the primary sources for this binding process between subunits. For homotetrameric proteins such as Sorbitol dehydrogenase(SDH), the structure is believed to have evolved going from a monomeric to a dimeric and finally a tetrameric structure in evolution. The binding process in SDH and many other tetrameric enzymes can be described by the gain in free energy which can be determined from the rate of association and dissociation. The following image shows the assembly of the four subunits (A,B,C and D) in SDH.

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