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  2. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    In practice, a protein with an excess of basic aminoacids (arginine, lysine and/or histidine) will bear an isoelectric point roughly greater than 7 (basic), while a protein with an excess of acidic aminoacids (aspartic acid and/or glutamic acid) will often have an isoelectric point lower than 7 (acidic).

  3. 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 ...

  4. Deamidation - Wikipedia

    en.wikipedia.org/wiki/Deamidation

    Asn-Gly (NG),is the most flexible and since it is acidic, it is most prone to deamidation with a half-life around 24 h under physiological conditions (pH 7.4, 37 °C). [3] As a free amino acid, or as the N-terminal residue of a peptide or protein, glutamine deamidates readily to form pyroglutamic acid (5-oxoproline). The reaction proceeds via ...

  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. Bicarbonate buffer system - Wikipedia

    en.wikipedia.org/wiki/Bicarbonate_buffer_system

    The pH of tears shift throughout a waking day, rising "about 0.013 pH units/hour" until a prolonged closed-eye period causes the pH to fall again. [15] Most healthy individuals have tear pH in the range of 7.0 to 7.7, where bicarbonate buffering is the most significant, but proteins and other buffering components are also present that are ...

  7. Aspartic acid - Wikipedia

    en.wikipedia.org/wiki/Aspartic_acid

    Aspartic acid has an acidic side chain (CH 2 COOH) which reacts with other amino acids, enzymes and proteins in the body. [5] Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged aspartate form, −COO −. [5] It is a non-essential amino acid in humans, meaning the body can synthesize it ...

  8. Lysine - Wikipedia

    en.wikipedia.org/wiki/Lysine

    Lysine ball and stick model spinning. Lysine (symbol Lys or K) [2] is an α-amino acid that is a precursor to many proteins.Lysine contains an α-amino group (which is in the protonated −NH + 3 form when the lysine is dissolved in water at physiological pH), an α-carboxylic acid group (which is in the deprotonated −COO − form when the lysine is dissolved in water at physiological pH ...

  9. pH - Wikipedia

    en.wikipedia.org/wiki/PH

    At 25 °C (77 °F), solutions of which the pH is less than 7 are acidic, and solutions of which the pH is greater than 7 are basic. Solutions with a pH of 7 at 25 °C are neutral (i.e. have the same concentration of H + ions as OH − ions, i.e. the same as pure water). The neutral value of the pH depends on the temperature and is lower than 7 ...

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