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    www.aol.com/games/play/masque-publishing/crossword

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  3. Polylysine - Wikipedia

    en.wikipedia.org/wiki/Polylysine

    The precursor amino acid lysine contains two amino groups, one at the α-carbon and one at the ε-carbon. Either can be the location of polymerization, resulting in α-polylysine or ε-polylysine. Polylysine is a homopolypeptide belonging to the group of cationic polymers: at pH 7, polylysine contains a positively charged hydrophilic amino group.

  4. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Codon–amino acids mappings may be the biological information system at the primordial origin of life on Earth. [128] While amino acids and consequently simple peptides must have formed under different experimentally probed geochemical scenarios, the transition from an abiotic world to the first life forms is to a large extent still unresolved ...

  5. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)

  6. Amino radical - Wikipedia

    en.wikipedia.org/wiki/Amino_radical

    In chemistry, the amino radical, ·NH 2, also known as the aminyl or azanyl, is the neutral form of the amide ion (NH − 2). Aminyl radicals are highly reactive and consequently short-lived, like most radicals; however, they form an important part of nitrogen chemistry. In sufficiently high concentration, amino radicals dimerise to form hydrazine.

  7. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    In a hydrophilic environment such as cytosol, the hydrophobic amino acids will concentrate at the core of the protein, while the hydrophilic amino acids will be on the exterior. This is entropically favorable since water molecules can move much more freely around hydrophilic amino acids than hydrophobic amino acids.

  8. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    In addition to the common amino acid L-tyrosine, which is the para isomer (para-tyr, p-tyr or 4-hydroxyphenylalanine), there are two additional regioisomers, namely meta-tyrosine (also known as 3-hydroxyphenylalanine, L-m-tyrosine, and m-tyr) and ortho-tyrosine (o-tyr or 2-hydroxyphenylalanine), that occur in nature.

  9. Glycine - Wikipedia

    en.wikipedia.org/wiki/Glycine

    Glycine (symbol Gly or G; [6] / ˈ ɡ l aɪ s iː n / ⓘ) [7] is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable). Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). [8]

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