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  2. Histidine - Wikipedia

    en.wikipedia.org/wiki/Histidine

    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 protonated), classifying it as a ...

  3. 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]

  4. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    The isoelectric point (pI, pH(I), IEP), is the pH at which a molecule carries no net electrical charge or is electrically neutral in the statistical mean. The standard nomenclature to represent the isoelectric point is pH(I). [ 1 ]

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Arginine has a charged guanidino group and lysine a charged alkyl amino group, and are fully protonated at pH 7. Histidine's imidazole group has a pK a of 6.0, and is only around 10% protonated at neutral pH. Because histidine is easily found in its basic and conjugate acid forms it often participates in catalytic proton transfers in enzyme ...

  6. Salt bridge (protein and supramolecular) - Wikipedia

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

    The midpoint of the titration curve corresponds to the pK a, or the pH where the ratio of protonated: deprotonated molecules is 1:1. Continuing with the T4 lysozyme example, a titration curve is obtained through observation of a shift in the C2 proton of histidine 31 (Figure 5).

  7. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    The strong charge makes these two amino acids prone to be located on the outer hydrophilic surfaces of the proteins; when they are found inside, they are usually paired with a corresponding negatively charged amino acid, e.g., aspartate or glutamate. Leucine: L Leu Leu is essential for humans, and behaves similarly to isoleucine and valine ...

  8. Acid–base homeostasis - Wikipedia

    en.wikipedia.org/wiki/Acid–base_homeostasis

    Acid–base homeostasis is the homeostatic regulation of the pH of the body's extracellular fluid (ECF). [1] The proper balance between the acids and bases (i.e. the pH) in the ECF is crucial for the normal physiology of the body—and for cellular metabolism. [1]

  9. Intracellular pH - Wikipedia

    en.wikipedia.org/wiki/Intracellular_pH

    Physiologically normal intracellular pH is most commonly between 7.0 and 7.4, though there is variability between tissues (e.g., mammalian skeletal muscle tends to have a pH i of 6.8–7.1). [4] [5] There is also pH variation across different organelles, which can span from around 4.5 to 8.0. [6] [7] pH i can be measured in a number of ...