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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]
Collagen (/ ˈ k ɒ l ə dʒ ə n /) is the main structural protein in the extracellular matrix of the connective tissues of many animals. It is the most abundant protein in mammals, [1] making up 25% to 35% of protein content. Amino acids are bound together to form a triple helix of elongated fibril [2] known as a 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.
Furthermore, proline is rarely found in α and β structures as it would reduce the stability of such structures, because its side chain α-nitrogen can only form one nitrogen bond. Additionally, proline is the only amino acid that does not form a red-purple colour when developed by spraying with ninhydrin for uses in chromatography. Proline ...
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.
The global protein supplement market was valued at $5.8 billion in 2022, with a projected 8% compound annual growth rate through 2030, according to Grand View Research. Below, Levinson and other ...
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 ...
Proline: P Pro Pro contains an unusual ring to the N-end amine group, which forces the CO-NH amide sequence into a fixed conformation. It can disrupt protein folding structures like α helix or β sheet, forcing the desired kink in the protein chain. Common in collagen, it often undergoes a post-translational modification to hydroxyproline ...
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