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Affinity chromatography is a method of separating a biomolecule from a mixture, based on a highly specific macromolecular binding interaction between the biomolecule and another substance.
Membrane attack complex (Terminal complement complex C5b-9) A membrane attack complex attached to a pathogenic cell The membrane attack complex (MAC) or terminal complement complex (TCC) is a complex of proteins typically formed on the surface of pathogen cell membranes as a result of the activation of the host's complement system, and as such is an effector of the immune system.
In biochemistry, isomerases are a general class of enzymes that convert a molecule from one isomer to another. Isomerases facilitate intramolecular rearrangements in which bonds are broken and formed. The general form of such a reaction is as follows:
Many biological circuits produce complex outputs by exploiting one or more feedback loops. In a sequence of biochemical events, feedback would refer to a downstream element in the sequence (B in the adjacent image) affecting some upstream component (A in the adjacent image) to affect its own production or activation (output) in the future.
In biochemistry and pharmacology, receptors are chemical structures, composed of protein, that receive and transduce signals that may be integrated into biological systems. [1] These signals are typically chemical messengers [nb 1] which bind to a receptor and produce physiological responses such as change in the electrical activity of a cell.
In a biochemistry that used sulfuric acid as a solvent, the alkene group (C=C), with two carbon atoms joined by a double bond, could function analogously to the carbonyl group (C=O) in water-based biochemistry. [43] A proposal has been made that life on Mars may exist and be using a mixture of water and hydrogen peroxide as its solvent. [79]
iCLIP [1] [2] [3] (individual-nucleotide resolution crossLinking and immunoprecipitation) is a variant of the original CLIP method used for identifying protein-RNA interactions, [4] which uses UV light to covalently bind proteins and RNA molecules to identify RNA binding sites of proteins.
The class I amidotransferase domain is made of the N terminal 206 residues of the enzyme, and consists of 12 beta strands and 5 alpha helices; the core of this domain is an open 7-stranded mixed beta sheet. Its catalytic triad includes Cys86, His181 and Glu183.