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  2. 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.

  3. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    E.g., DNA-binding proteins have their active regions rich with arginine and lysine. 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

  4. Lysine - Wikipedia

    en.wikipedia.org/wiki/Lysine

    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), and a side chain (CH 2) 4 NH 2 (which ...

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2] Only these 22 appear in the genetic code of life. [3][4]

  6. 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.

  7. Essential amino acid - Wikipedia

    en.wikipedia.org/wiki/Essential_amino_acid

    Essential amino acid. An essential amino acid, or indispensable amino acid, is an amino acid that cannot be synthesized from scratch by the organism fast enough to supply its demand, and must therefore come from the diet. Of the 21 amino acids common to all life forms, the nine amino acids humans cannot synthesize are valine, isoleucine ...

  8. Hydrophilicity plot - Wikipedia

    en.wikipedia.org/wiki/Hydrophilicity_plot

    Hydrophilicity plot. A hydrophilicity plot is a quantitative analysis of the degree of hydrophobicity or hydrophilicity of amino acids of a protein. It is used to characterize or identify possible structure or domains of a protein. The plot has amino acid sequence of a protein on its x-axis, and degree of hydrophobicity and hydrophilicity on ...

  9. Aquaporin - Wikipedia

    en.wikipedia.org/wiki/Aquaporin

    The aromatic/arginine or "ar/R" selectivity filter is a cluster of amino acids that help bind to water molecules and exclude other molecules that may try to enter the pore. It is the mechanism by which the aquaporin is able to selectively bind water molecules and so to allow them through, and to prevent other molecules from entering.