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  2. Phenylalanine - Wikipedia

    en.wikipedia.org/wiki/Phenylalanine

    Phenylalanine (symbol Phe or F) [3] is an essential α-amino acid with the formula C 9 H 11 NO 2.It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine.

  3. Hydrophobic effect - Wikipedia

    en.wikipedia.org/wiki/Hydrophobic_effect

    The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and to be excluded by water. [1][2] The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes the entropy of water and minimizes the area of contact between ...

  4. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    While tyrosine is generally classified as a hydrophobic amino acid, it is more hydrophilic than phenylalanine. [5] It is encoded by the codons UAC and UAU in messenger RNA. The one-letter symbol Y was assigned to tyrosine for being alphabetically nearest of those letters available.

  5. Phenylalanine: Role of Amino Acid and Purpose in Diet

    www.aol.com/phenylalanine-role-amino-acid...

    Phenylalanine is an essential amino acid that most of us get more than enough of through protein sources in our everyday diets, whether we eat mostly animal-derived, plant-based, or a mix of both.

  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. Proteinogenic amino acid - Wikipedia

    en.wikipedia.org/wiki/Proteinogenic_amino_acid

    Phenylalanine: F Phe Essential for humans, phenylalanine, tyrosine, and tryptophan contain a large, rigid aromatic group on the side chain. These are the biggest amino acids. Like isoleucine, leucine, and valine, these are hydrophobic and tend to orient towards the interior of the folded protein molecule. Phenylalanine can be converted into ...

  8. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Glycine and proline are strongly present within low complexity regions of both eukaryotic and prokaryotic proteins, whereas the opposite is the case with cysteine, phenylalanine, tryptophan, methionine, valine, leucine, isoleucine, which are highly reactive, or complex, or hydrophobic. [40] [42] [43]

  9. Aromatic amino acid - Wikipedia

    en.wikipedia.org/wiki/Aromatic_amino_acid

    In plants, the shikimate pathway first leads to the formation of chorismate, which is the precursor of phenylalanine, tyrosine, and tryptophan.These aromatic amino acids are the precursors of many secondary metabolites, all essential to a plant's biological functions, such as the hormones salicylate and auxin.