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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    There are three amino acids with side chains that are cations at neutral pH: arginine (Arg, R), lysine (Lys, K) and histidine (His, H). Arginine has a charged guanidino group and lysine a charged alkyl amino group, and are fully protonated at pH 7.

  3. Pleckstrin homology domain - Wikipedia

    en.wikipedia.org/wiki/Pleckstrin_homology_domain

    Pleckstrin homology domain(PH domain) or (PHIP) is a protein domainof approximately 120 amino acidsthat occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton. [1][2][3][4][5][6][7] This domain can bind phosphatidylinositollipids within biological membranes (such as phosphatidylinositol (3 ...

  4. Tryptophan - Wikipedia

    en.wikipedia.org/wiki/Tryptophan

    Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (– NH + 3; pK a = 9.39) and the carboxylic acid is deprotonated ( –COO −; pK a = 2.38). [5] Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid.

  5. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Hydrophobicity scales. Hydrophobicity scales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more hydrophobic are the amino acids located in that region of the protein. These scales are commonly used to predict the transmembrane alpha-helices of membrane proteins.

  6. Arginine - Wikipedia

    en.wikipedia.org/wiki/Arginine

    Arginine is the amino acid with the formula (H 2 N)(HN)CN(H)(CH 2) 3 CH(NH 2)CO 2 H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO 2 −) and both the amino and guanidino groups are protonated, resulting in a cation.

  7. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...

  8. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    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] However, pI is also used. [ 2] For brevity, this article uses pI.

  9. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    The table below lists the abundance of amino acids in E.coli cells and the metabolic cost (ATP) for synthesis of the amino acids. Negative numbers indicate the metabolic processes are energy favorable and do not cost net ATP of the cell. [12] The abundance of amino acids includes amino acids in free form and in polymerization form (proteins).

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