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Collagen has an unusual amino acid composition and sequence: Glycine is found at almost every third residue. Proline makes up about 17% of collagen. Collagen contains two unusual derivative amino acids not directly inserted during translation. These amino acids are found at specific locations relative to glycine and are modified post ...
Hydroxylysine (Hyl) is an amino acid with the molecular formula C 6 H 14 N 2 O 3. It was first discovered in 1921 by Donald Van Slyke as the 5-hydroxylysine form. [1] It arises from a post-translational hydroxy modification of lysine. It is most widely known as a component of collagen. [2] It is biosynthesized from lysine via oxidation by lysyl ...
This mutation substitutes the amino acid cysteine for the amino acid arginine at position 134 in the protein made by the gene. (The mutation can also be written as Arg134Cys.) The altered protein interacts abnormally with other collagen-building proteins, disrupting the structure of type I collagen fibrils and trapping collagen in the cell.
Type I collagen is the most abundant collagen of the human body, consisting of around 90% of the body's total collagen in vertebrates. Due to this, it is also the most abundant protein type found in all vertebrates. Type I forms large, eosinophilic fibers known as collagen fibers, which make up most of the rope-like dense connective tissue in ...
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Hydroxyproline and proline play key roles for collagen stability. [4] They permit the sharp twisting of the collagen helix. [5] In the canonical collagen Xaa-Yaa-Gly triad (where Xaa and Yaa are any amino acid), a proline occupying the Yaa position is hydroxylated to give a Xaa-Hyp-Gly sequence.