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  2. Hydroxyproline - Wikipedia

    en.wikipedia.org/wiki/Hydroxyproline

    Hydroxyproline is a major component of the protein collagen, [3] comprising roughly 13.5% of mammalian collagen. Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5]

  3. 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.

  4. Triple helix - Wikipedia

    en.wikipedia.org/wiki/Triple_helix

    The collagen peptide is composed of repeats of Gly-X-Y, with the second residue (X) usually being Pro and the third (Y) being hydroxyproline. [6] [5] A DNA triple helix is made up of three separate DNA strands, each oriented with the sugar/phosphate backbone on the outside of the helix and the bases on the inside of the helix.

  5. Proline - Wikipedia

    en.wikipedia.org/wiki/Proline

    Proline (symbol Pro or P) [4] is an organic acid classed as a proteinogenic amino acid (used in the biosynthesis of proteins), although it does not contain the amino group-NH 2 but is rather a secondary amine.

  6. Systemin - Wikipedia

    en.wikipedia.org/wiki/Systemin

    In 2001, biologically active hydroxyproline-rich glycopeptides were isolated from tobacco which activated the production of protease inhibitors in a similar way to systemin in tomatoes. [1] Although they are structurally unrelated to systemins, their similar function resulted in them being named hydroxyproline-rich systemins (HypSys).

  7. Secondary amino acid - Wikipedia

    en.wikipedia.org/wiki/Secondary_amino_acid

    In nature, proline, hydroxyproline, pipecolic acid and sarcosine are well-known secondary amino acids. Proline is the only proteinogenic secondary amino acids. Other secondary amino acids are non-proteinogenic amino acids. In protein, hydroxyproline is incorporated into protein by hydroxylation of proline.

  8. Collagen hybridizing peptide - Wikipedia

    en.wikipedia.org/wiki/Collagen_Hybridizing_Peptide

    Schematic of a CHP strand (labeled with an "X" tag) hybridizing to denatured collagen chains and forming a collagen triple helix. During disease progression, tissue development, or ageing, collagen can be extensively degraded by collagenolytic proteases, causing its triple helix to unfold at the physiological temperature due to reduced thermal stability.

  9. Molecular Structure of Nucleic Acids: A Structure for ...

    en.wikipedia.org/wiki/Molecular_Structure_of...

    The two base-pair complementary chains of the DNA molecule allow replication of the genetic instructions. The "specific pairing" is a key feature of the Watson and Crick model of DNA, the pairing of nucleotide subunits. [5] In DNA, the amount of guanine is equal to cytosine and the amount of adenine is equal to thymine. The A:T and C:G pairs ...

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