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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. His-tag - Wikipedia

    en.wikipedia.org/wiki/His-tag

    Subsequent studies have revealed that among amino acids constituting proteins, histidine is strongly involved in the coordination complex with metal ions. [4] Therefore, if a number of histidines are added to the end of the protein, the affinity of the protein for the metal ion is increased and this can be exploited to selectively isolate the ...

  4. Catalytic triad - Wikipedia

    en.wikipedia.org/wiki/Catalytic_triad

    The positive charge on the basic residue is simultaneously stabilised, leading to its polarisation. [3] Two amino acids have acidic side chains at physiological pH (aspartate or glutamate) and so are the most common members of the acidic triad residue. [ 3 ]

  5. Histatin - Wikipedia

    en.wikipedia.org/wiki/Histatin

    The structure of histatin is unique depending on whether the protein of interest is histatin 1, 3 or 5. Nonetheless, histatins mainly possess a cationic (positive) charge due to the primary structure consisting mostly of basic amino acids. An amino acid that is crucial to histatin's function is histidine.

  6. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    In nonpolar solvents contact ion pairs with very high association constants are formed; [3] [4] in the gas phase the association energies of e.g. alkali halides reach up to 200 kJ/mol. [5] The Bjerrum or the Fuoss equation describe ion pair association as function of the ion charges zA and zB and the dielectric constant ε of the medium; a ...

  7. Cation–π interaction - Wikipedia

    en.wikipedia.org/wiki/Cation–π_interaction

    Similar to these other non-covalent bonds, cation–π interactions play an important role in nature, particularly in protein structure, molecular recognition and enzyme catalysis. The effect has also been observed and put to use in synthetic systems. [1] [2] The π system above and below the benzene ring leads to a quadrupole charge distribution.

  8. Affinity chromatography - Wikipedia

    en.wikipedia.org/wiki/Affinity_chromatography

    Histidine tags have an affinity for nickel, cobalt, zinc, copper and iron ions which have been immobilized by forming coordinate covalent bonds with a chelator incorporated in the stationary phase. For elution, an excess amount of a compound able to act as a metal ion ligand, such as imidazole, is used. GST has an affinity for glutathione which ...

  9. Histidine (data page) - Wikipedia

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

    Chemical formula: C 6 H 9 N 3 O 2 Molar mass: 155.16 g·mol −1 Systematic name: 2-amino-3-(3H-imidazol-4-yl)propanoic acid Abbreviations: H, His Synonyms: Imidazole alanine ({S/D})-α-amino-1H-imidazole-4-propanoic acid