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| tetrameric protein ： ウィキペディア英語版 |
tetrameric protein
A tetramer is a protein with a quaternary structure of four subunits (tetrameric). Homotetramers have four identical subunits (such as glutathione S-transferase), dimers of dimers contain two heterodimer subunits (such as hemoglobin), and heterotetramers are complexes of four different subunits.
==Subunit interactions in tetramers==
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.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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