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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]
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 ...
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 ]
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.
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 ...
They noted that most researchers were using acute methods of cholesterol depletion, which disrupt the rafts, but also disrupt another lipid known as PI(4,5)P 2. PI(4,5)P 2 plays a large role in regulating the cell's cytoskeleton , [ 72 ] and disrupting PI(4,5)P 2 causes many of the same results as this type of cholesterol depletion, including ...
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.
Tetramer variants have been developed that, either radiolabelled or coupled to a toxin such as saporin, can be injected into live mice to modulate or even deplete specific T cell populations. [ 19 ] [ 20 ] Peptide–MHC tetramers have also been used therapeutically. [ 21 ]