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A tetramer (/ ˈ t ɛ t r ə m ər /) (tetra-, "four" + -mer, "parts") is an oligomer formed from four monomers or subunits. The associated property is called tetramery . An example from inorganic chemistry is titanium methoxide with the empirical formula Ti(OCH 3 ) 4 , which is tetrameric in solid state and has the molecular formula Ti 4 (OCH ...
The heterotetrameric molecule haemoglobin, made up of four subunits of two different types (coloured red and blue.) A homotetramer is a protein complex made up of four identical subunits which are associated but not covalently bound. [3] Conversely, a heterotetramer is a 4-subunit complex where one or more subunits differ. [4]
Pentamers consist of five MHC-peptide headgroups, arranged in a planar configuration so that, unlike MHC tetramers, all of the headgroups can contact the CD8+ T cell. The headgroups are connected via flexible linkers to a coiled-coil multimerization domain, which in turn is connected to five fluorescent or biotin tags.
For example, a tetrameric protein may have one four-fold rotation axis, i.e. point group symmetry 4 or C 4. In this case the four interfaces between the subunits are identical. It may also have point group symmetry 222 or D 2. This tetramer has different interfaces and the tetramer can dissociate into two identical homodimers.
In chemistry and biochemistry, an oligomer (/ ə ˈ l ɪ ɡ ə m ər / ⓘ) is a molecule that consists of a few repeating units which could be derived, actually or conceptually, from smaller molecules, monomers. [1] [2] [3] The name is composed of Greek elements oligo-, "a few" and -mer, "parts". An adjective form is oligomeric. [3]
Specifically it would be called a dimer if it contains two subunits, a trimer if it contains three subunits, a tetramer if it contains four subunits, and a pentamer if it contains five subunits, and so forth. The subunits are frequently related to one another by symmetry operations, such as a 2-fold axis in a dimer.
DNA gyrase is a tetrameric enzyme that consists of 2 GyrA ("A") and 2 GyrB ("B") subunits. [8] Structurally the complex is formed by 3 pairs of "gates", sequential opening and closing of which results into the direct transfer of DNA segment and introduction of 2 negative supercoils. N-gates are formed by ATPase domains of GyrB subunits.
Hemoglobin Gower 2 (also referred to as α 2 ε 2 or HbE Gower-2) is a form of hemoglobin existing at low levels during embryonic and fetal life. It is composed of two alpha chains and two epsilon chains, and is somewhat unstable, though not as much as hemoglobin Gower 1. [ 4 ]