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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 3 ...
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]
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.
A central pore, 10 Å wide, is located near the center of the transmembrane channel, where the energy barrier is highest for the transversing ion due to the hydrophobity of the channel wall. The water-filled cavity and the polar C-terminus of the pore helices ease the energetic barrier for the ion.
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]
The nucleosome core particle consists of approximately 146 base pairs (bp) of DNA [11] wrapped in 1.67 left-handed superhelical turns around a histone octamer, consisting of 2 copies each of the core histones H2A, H2B, H3, and H4. [12] Core particles are connected by stretches of linker DNA, which can be up to about 80 bp long.
The size of the cavity contributes to the size of the particle that the cavity can enclose, for example inorganic nanoparticles, nucleic acids, and even other proteins. [6] The interior or chamber portion of the protein cage is usually accessible through a pore which is located in between protein subunits.