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The collagen protein is composed of a triple helix, which generally consists of two identical chains (α1) and an additional chain that differs slightly in its chemical composition (α2). [23] The amino acid composition of collagen is atypical for proteins, particularly with respect to its high hydroxyproline content.
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 ...
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.
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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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