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Collagen consists of amino acids bound together to form a triple helix of elongated fibril [2] known as a collagen helix. It is mostly found in connective tissue such as cartilage, bones, tendons, ligaments, and skin. Vitamin C is vital for collagen synthesis, and Vitamin E improves the production of collagen.
Type II collagen is the basis for hyaline cartilage, including the articular cartilages at joint surfaces. It is formed by homotrimers of collagen, type II, alpha 1 chains. It makes up 50% of all protein in cartilage and 85–90% of collagen of articular cartilage. Type II collagen is organised into fibrils. This fibrillar network of collagen ...
Swiss-model. Domains. InterPro. 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 ...
Type III Collagen is a homotrimer, or a protein composed of three identical peptide chains (), each called an alpha 1 chain of type III collagen.Formally, the monomers are called collagen type III, alpha-1 chain and in humans are encoded by the COL3A1 gene.Type III collagen is one of the fibrillar collagens whose proteins have a long, inflexible, triple-helical domain.
- COL3A1, EDS4A, collagen type III alpha 1, collagen type III alpha 1 chain, EDSVASC, PMGEDSV
Anchoring fibrils. Anchoring fibrils (composed largely of type VII collagen) extend from the basal lamina of epithelial cells and attach to the lamina reticularis (also known as the reticular lamina) by wrapping around the reticular fiber ( collagen III) bundles. The basal lamina and lamina reticularis together make up the basement membrane.
Pneumonoultramicroscopicsilicovolcanoconiosis is the longest word in the English language. The word can be analysed as follows: This word was invented in the daily meeting from the National Puzzlers' League (N.P.L.) by its president Everett M. Smith. The word featured in the headline for an article published by the New York Herald ...
The serpin (white) first binds a protease (grey) with the exposed reactive centre loop (blue). When this loop is cleaved by the protease, it rapidly inserts into the A-sheet (light blue), deforming and inhibiting the protease. ( PDB: 1K9O, 1EZX ) Serine and cysteine proteases operate by a two-step catalytic mechanism.