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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The last of the 20 common amino acids to be discovered was threonine in 1935 by William Cumming Rose, who also determined the essential amino acids and established the minimum daily requirements of all amino acids for optimal growth. [15] [16] The unity of the chemical category was recognized by Wurtz in 1865, but he gave no particular name to ...

  3. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    It is a non-essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. [3][4] It is called tyrosyl when referred to as a functional group or side chain.

  4. Aromatic amino acid - Wikipedia

    en.wikipedia.org/wiki/Aromatic_amino_acid

    Aromatic amino acids, excepting histidine, absorb ultraviolet light above and beyond 250 nm and will fluoresce under these conditions. This characteristic is used in quantitative analysis, notably in determining the concentrations of these amino acids in solution. [1] [2] Most proteins absorb at 280 nm due to the presence of tyrosine and ...

  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. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino -terminal (N) end to the carboxyl -terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells.

  7. Glutamine - Wikipedia

    en.wikipedia.org/wiki/Glutamine

    Glutamine (data page) Glutamine (symbol Gln or Q) [4] is an α-amino acid that is used in the biosynthesis of proteins. Its side chain is similar to that of glutamic acid, except the carboxylic acid group is replaced by an amide. It is classified as a charge-neutral, polar amino acid.

  8. List of amino acids - Wikipedia

    en.wikipedia.org/wiki/List_of_amino_acids

    Appearance. move to sidebarhide. From Wikipedia, the free encyclopedia. Amino acids are listed by type: Proteinogenic amino acid. Non-proteinogenic amino acids. Topics referred to by the same term. This disambiguationpage lists articles associated with the title List of amino acids. If an internal linkled you here, you may wish to change the ...

  9. 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.