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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 ...
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.
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]
Hydrogen bonding networks between subunits has been shown to be important for the stability of the tetrameric quaternary protein structure.For example, a study of SDH which used diverse methods such as protein sequence alignments, structural comparisons, energy calculations, gel filtration experiments and enzyme kinetics experiments, could reveal an important hydrogen bonding network which ...
The number of subunits in a protein complex can often be determined by measuring the hydrodynamic molecular volume or mass of the intact complex, which requires native solution conditions. For folded proteins, the mass can be inferred from its volume using the partial specific volume of 0.73 ml/g.
Like other crown ethers, 12-crown-4 complexes with alkali metal cations. The cavity diameter of 1.2-1.5 Å gives it a high selectivity towards the lithium cation (ionic diameter 1.36 Å) [2] Its point group is S 4. The dipole moment of 12-crown-4 varies with solvent and temperature.
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.
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 ...