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  2. Metalloprotein - Wikipedia

    en.wikipedia.org/wiki/Metalloprotein

    The presence of the metal ion allows metalloenzymes to perform functions such as redox reactions that cannot easily be performed by the limited set of functional groups found in amino acids. [16] The iron atom in most cytochromes is contained in a heme group. The differences between those cytochromes lies in the different side-chains.

  3. Collagen - Wikipedia

    en.wikipedia.org/wiki/Collagen

    A distinctive feature of collagen is the regular arrangement of amino acids in each of the three chains of these collagen subunits. The sequence often follows the pattern Gly-Pro-X or Gly-X-Hyp, where X may be any of various other amino acid residues. [24] Proline or hydroxyproline constitute about 1/6 of the total sequence.

  4. Collagen, type I, alpha 1 - Wikipedia

    en.wikipedia.org/wiki/Collagen,_type_I,_alpha_1

    Other mutations cause the amino acid glycine to be replaced by a different amino acid in the pro-alpha1(I) chain, which inhibits the essential interaction between protein chains. Type I collagen production is inhibited by the inability of the altered procollagen strands to associate and form the triple-stranded, ropelike structure of mature ...

  5. Type I collagen - Wikipedia

    en.wikipedia.org/wiki/Type_I_collagen

    Chemical Structure of Type I Collagen. Type I collagen has a triple-helical form which is caused by its amino acid composition. Its specific domain follows an order of G-X-Y In which the X and Y slots are occupied by any amino acid other than glycine however these slots are typically occupied by both hydroxyproline and proline, not in any particular order. [5]

  6. Collagen, type III, alpha 1 - Wikipedia

    en.wikipedia.org/wiki/Collagen,_type_III,_alpha_1

    1281 12825 Ensembl ENSG00000168542 ENSMUSG00000026043 UniProt P02461 P08121 RefSeq (mRNA) NM_000090 NM_001376916 NM_009930 RefSeq (protein) NP_000081 NP_034060 Location (UCSC) Chr 2: 188.97 – 189.01 Mb Chr 1: 45.35 – 45.39 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Type III Collagen is a homotrimer, or a protein composed of three identical peptide chains (monomers), each ...

  7. 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 ...

  8. Transition metal amino acid complexes - Wikipedia

    en.wikipedia.org/wiki/Transition_metal_amino...

    Transition metal amino acid complexes are a large family of coordination complexes containing the conjugate bases of the amino acids, the 2-aminocarboxylates. Amino acids are prevalent in nature, and all of them function as ligands toward the transition metals. [1] Not included in this article are complexes of the amides (including peptide) and ...

  9. Collagen helix - Wikipedia

    en.wikipedia.org/wiki/Collagen_helix

    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. Collagen triple helices are often bundled into fibrils which themselves form larger fibres, as in tendons.