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Histidine ball and stick model spinning. Histidine (symbol His or H) [2] is an essential amino acid that is used in the biosynthesis of proteins.It contains an α-amino group (which is in the protonated –NH 3 + form under biological conditions), a carboxylic acid group (which is in the deprotonated –COO − form under biological conditions), and an imidazole side chain (which is partially ...
Most commonly, a polyhistidine tag is fused at the N-terminus or C-terminus of a protein and is attached via a short flexible linker, which may contain a protease cleavage site. [ 10 ] [ 9 ] Less commonly, tags can be added at both the N- and C-termini or inserted at an intermediate part of a protein, such as within an exposed loop.
The triad is exemplified by chymotrypsin, [c] a model serine protease from the PA superfamily which uses its triad to hydrolyse protein backbones. The aspartate is hydrogen bonded to the histidine, increasing the pK a of its imidazole nitrogen from 7 to around 12. Histidine is thus able to act as a powerful general base, activating the serine ...
In phosphorelays, the "hybrid" histidine kinase contains an internal aspartate-containing receiver domain to which the phosphoryl group is transferred, after which an HPt protein containing a phosphorylatable histidine receives the phosphoryl group and finally transfers it to the response regulator.
In terms of enzymology, a histidine kinase (EC 2.7.13.3, EnvZ, histidine protein kinase, protein histidine kinase, protein kinase (histidine), HK1, HP165, Sln1p) is an enzyme that catalyzes the chemical reaction. ATP + protein L-histidine ADP + protein N-phospho-L-histidine.
Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...
Human myoglobin contains 154 amino acids. [35] Myoglobin contains a porphyrin ring with an iron at its center. A proximal histidine group (His-93) is attached directly to iron, and a distal histidine group (His-64) hovers near the opposite face. [35] The distal imidazole is not bonded to the iron, but is available to interact with the substrate ...
The crystal structure of the yeast histidine phosphotransfer protein Ypd1 in complex with the response regulator Sln1. Ypd1 appears on the right with the conserved four-helical bundle in yellow and variable helices in red. Sln1 appears on the left with beta sheets in tan and helices in brown.