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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.
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.
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.
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]
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 A (HbA), also known as adult hemoglobin, hemoglobin A1 or α 2 β 2, is the most common human hemoglobin tetramer, accounting for over 97% of the total red blood cell hemoglobin. [1] Hemoglobin is an oxygen-binding protein, found in erythrocytes , which transports oxygen from the lungs to the tissues. [ 2 ]