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  2. Cyclic glycine-proline - Wikipedia

    en.wikipedia.org/wiki/Cyclic_glycine-proline

    Cyclic glycine-proline (cGP) is a small neuroactive peptide that belongs to a group of bioactive 2,5-diketopiperazines (2,5-DKPs) and is also known as cyclo-glycine-proline. cGP is a neutral, stable naturally occurring compound and is endogenous to the human body; found in human plasma, breast milk and cerebrospinal fluid.

  3. Proline - Wikipedia

    en.wikipedia.org/wiki/Proline

    The CBS reduction and proline catalysed aldol condensation are prominent examples. In brewing, proteins rich in proline combine with polyphenols to produce haze (turbidity). [25] L-Proline is an osmoprotectant and therefore is used in many pharmaceutical and biotechnological applications.

  4. 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).

  5. Collagen helix - Wikipedia

    en.wikipedia.org/wiki/Collagen_helix

    In 1954, Ramachandran & Kartha (13, 14) advanced a structure for the collagen triple helix on the basis of fiber diffraction data. It consists of a triple helix made of the repetitious amino acid sequence glycine-X-Y, where X and Y are frequently proline or hydroxyproline. [2] [3] Collagen folded into a triple helix is known as tropocollagen.

  6. Prolamin - Wikipedia

    en.wikipedia.org/wiki/Prolamin

    Prolamins are a group of plant storage proteins having a high proline amino acid content. They are found in plants, mainly in the seeds of cereal grains such as wheat , barley , rye , corn , sorghum , and oats . They are characterised by a high glutamine and proline content, and have poor solubility in water. They solubilise best in strong ...

  7. Low complexity regions in proteins - Wikipedia

    en.wikipedia.org/wiki/Low_complexity_regions_in...

    Tandem repeats of short oligopeptides that are rich in glycine, proline, serine or threonine are capable of forming flexible structures that bind ligands under certain pH and temperature conditions. [6] Proline is a well-known alpha-helix breaker, however, amino acid repeats composed of proline may form poly-proline helices. [7]

  8. Secondary amino acid - Wikipedia

    en.wikipedia.org/wiki/Secondary_amino_acid

    In protein, hydroxyproline is incorporated into protein by hydroxylation of proline. Pipecolic acid, a heavier analog of proline, is found in efrapeptin. Sarcosine is a N-methylized glycine so its methyl group is used in many biochemical reactions. Azetidine-2-carboxylic acid, which is a smaller homolog of proline in plants.

  9. Polyproline helix - Wikipedia

    en.wikipedia.org/wiki/Polyproline_helix

    A polyproline helix is a type of protein secondary structure which occurs in proteins comprising repeating proline residues. [1] A left-handed polyproline II helix (PPII, poly-Pro II, κ-helix [2]) is formed when sequential residues all adopt (φ,ψ) backbone dihedral angles of roughly (-75°, 150°) and have trans isomers of their peptide bonds.