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  2. 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. Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). [8]

  3. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Also, amino acid side chain affinity for water was measured using vapor phases. [14] Vapor phases represent the simplest non polar phases, because it has no interaction with the solute. [18] The hydration potential and its correlation to the appearance of amino acids on the surface of proteins was studied by Wolfenden.

  4. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Glycine (Gly, G) could be considered a polar amino acid since its small size means that its solubility is largely determined by the amino and carboxylate groups. However, the lack of any side chain provides glycine with a unique flexibility among amino acids with large ramifications to protein folding. [ 32 ]

  5. Serine - Wikipedia

    en.wikipedia.org/wiki/Serine

    It contains an α-amino group (which is in the protonated − NH + 3 form under biological conditions), a carboxyl group (which is in the deprotonated − COO − form under biological conditions), and a side chain consisting of a hydroxymethyl group, classifying it as a polar amino acid. It can be synthesized in the human body under normal ...

  6. Talk:Glycine - Wikipedia

    en.wikipedia.org/wiki/Talk:Glycine

    "The polar, uncharged amino acids except for glycine contain R groups, that can form hydrogen bonds with water. Thus, these amino acids are usually more soluble that non-polar amino acids." It continues later on "Glycine, the simplest amino acid, has only a single hydrogen for an R group, and this hydrogen is not a good hydrogen bond former.

  7. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    The N-O distance required is less than 4 Å (400 pm). Amino acids greater than this distance apart do not qualify as forming a salt bridge. [11] Due to the numerous ionizable side chains of amino acids found throughout a protein, the pH at which a protein is placed is crucial to its stability.

  8. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    Short pieces of left-handed helix sometimes occur with a large content of achiral glycine amino acids, but are unfavorable for the other normal, biological L-amino acids. The pitch of the alpha-helix (the vertical distance between consecutive turns of the helix) is 5.4 Å (0.54 nm), which is the product of 1.5 and 3.6.

  9. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein sequence is typically notated as a string of letters, listing the amino acids starting at the amino-terminal end through to the carboxyl-terminal end. Either a three letter code or single letter code can be used to represent the 22 naturally encoded amino acids, as well as mixtures or ambiguous amino acids (similar to nucleic acid ...