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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 formation of the sorbitol dehydrogenase tetramer from its monomers via dimers. A tetrameric protein is a protein with a quaternary structure of four subunits (tetrameric). Homotetramers have four identical subunits (such as glutathione S-transferase), and heterotetramers are complexes of different subunits.
A tetramer assay (also known as a tetramer stain) is a procedure that uses tetrameric proteins to detect and quantify T cells that are specific for a given antigen within a blood sample. [1] The tetramers used in the assay are made up of four major histocompatibility complex (MHC) molecules, which are found on the surface of most cells in the ...
This usually implies that the complex consists of different oligomerisation interfaces. 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.
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]
Structure of Saccharomyces cerevisiae TRiC in the AMP-PNP bound state (PDB 5GW5). [1]T-complex protein Ring Complex (TRiC), otherwise known as Chaperonin Containing TCP-1 (CCT), [a] is a multiprotein complex and the chaperonin of eukaryotic cells.
MOPs have cage-like frameworks with an enclosed cavity. The discrete self-assembly of metal ions and organic scaffolds to form MOPs into highly symmetrical architectures, is a modular process and has various applications. The self-assembly of various subunits that result in high symmetry is a common occurrence in biological systems.
The nucleosome assembles when DNA wraps around the histone octamer, two H2A-H2B dimers bound to an H3-H4 tetramer. The nucleosome core particle is the most basic form of DNA compaction in eukaryotes. Nucleosomes consist of a histone octamer surrounded by 146 base pairs of DNA wrapped in a superhelical manner. [10]