Histidine in a sentence

The pyruvate dehydrogenase family of kinases in animals is structurally related to histidine kinases, but instead phosphorylate serine residues, and probably do not use a phospho-histidine intermediate.

When the histidine is depleted only bacteria that have mutated to gain the ability to produce its own histidine will survive.

In 2015, his team developed an antibody to identify and study phosphates bonded to another amino acid called histidine.

Along with histidine 57 and aspartic acid 102, this serine residue constitutes the catalytic triad of the active site.

Also, histidine can donate a single carbon to THF to form methenyl-THF.

At the same time, the imidazole side-chain of the histidine residue interacting at the other pole of the iron is pulled toward the porphyrin ring.

Bacterial systems main * Ames test – This is the most commonly used test, and Salmonella typhimurium strains deficient in histidine biosynthesis are used in this test.

Binding also requires that alpha subunits contain a histidine amino acid residue, (i.

Here, a "tag" consisting of a specific amino acid sequence, often a series of histidine residues (a " His-tag "), is attached to one terminus of the protein.

High levels of phenolics in some woods can explain their natural preservation against rot. citation In plants, VirA is a protein histidine kinase which senses certain sugars and phenolic compounds.

Histidine kinases are also found in plants, fungi, animals, and other eukaryotes.

Iron's shift to a higher oxidation state in Hb-O 2 decreases the atom's size, and allows it into the plane of the porphyrin ring, pulling on the coordinated histidine residue and initiating the allosteric changes seen in the globulins.

The method tests the capability of the tested substance in creating mutations that result in a return to a "prototrophic" state, so that the cells can grow on a histidine-free medium.

These enzymes contain a catalytic triad consisting of histidine -57, aspartate -102, and serine -195. citation These three residues form a charge relay that increases nucleophilicity of the active site serine.

These strains are auxotrophic mutants, i.e. they require histidine for growth, but cannot produce it.

This ADP-ribosylation involves the transfer of an ADP-ribose from NAD+ to a diphthamide (a modified histidine ) residue within the EF-2 protein.

This causes the iron atom to move backward into the heme that holds it (the iron moves upward as it binds oxygen, in this illustration), tugging the histidine residue (modeled as a red pentagon on the right of the iron) closer, as it does.

This occurs via the concerted action of the three amino acid residues in the catalytic triad. citation Aspartate hydrogen bonds to the N-δ hydrogen of histidine, increasing the pKa of its ε nitrogen and thus making it able to deprotonate serine.

Unsaturated fatty acids can serve as the olefinic substrates for the ene reaction and unsaturated amino acids like histidine can be the reactant for the Diels–Alder cyclization.

When deoxyhemoglobin picks up an oxygen molecule, this histidine residue moves away and returns once the oxygen is securely attached to form a hydrogen bond with it.