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  2. Histidine - Wikipedia

    en.wikipedia.org/wiki/Histidine

    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 ...

  3. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    The triad of cytomegalovirus protease [b] uses histidine as both the acid and base triad members. Removing the acid histidine results in only a 10-fold activity loss (compared to >10,000-fold when aspartate is removed from chymotrypsin). This triad has been interpreted as a possible way of generating a less active enzyme to control cleavage ...

  4. Histidine (data page) - Wikipedia

    en.wikipedia.org/wiki/Histidine_(data_page)

    ^a CID 71083 from PubChem (D-histidine) ^a CID 6274 from PubChem (L-histidine) This page was last edited on 12 April 2023, at 11:40 (UTC). Text is ...

  5. Amino acid replacement - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_replacement

    Some amino acids are more likely to be replaced. One of the factors that influences this tendency is physicochemical distance. Example of a measure of amino acid can be Graur's Stability Index. [9] The assumption of this measure is that the amino acid replacement rate and protein's evolution is dependent on the amino acid composition of protein.

  6. His-tag - Wikipedia

    en.wikipedia.org/wiki/His-tag

    The total number of histidine residues may vary in the tag from as low as two, to as high as 10 or more His residues. N- or C-terminal His-tags may also be followed or preceded, respectively, by a suitable amino acid sequence that facilitates removal of the polyhistidine-tag using endopeptidases .

  7. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Polar chemical groups, such as OH group in methanol do not cause the hydrophobic effect. However, a pure hydrocarbon molecule, for example hexane, cannot accept or donate hydrogen bonds to water. Introduction of hexane into water causes disruption of the hydrogen bonding network between water molecules.

  8. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    Then the P-F bond is broken, one electron is transferred to the F atom and it leaves the intermediate as F − anion. It combines with a proton in solution to form one HF molecule. A covalent bond formed between the active site and DIFP, so the serine side chain is no longer available to the substrate. [17]

  9. Protein phosphorylation - Wikipedia

    en.wikipedia.org/wiki/Protein_phosphorylation

    Histidine and aspartate phosphorylation occurs in prokaryotes as part of two-component signaling and in some cases in eukaryotes in some signal transduction pathways. The analysis of phosphorylated histidine using standard biochemical and mass spectrometric approaches is much more challenging than that of Ser, Thr or Tyr.