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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 ...
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 ...
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.
A representation of the 3D structure of the protein myoglobin showing turquoise α-helices. This protein was the first to have its structure solved by X-ray crystallography. Toward the right-center among the coils, a prosthetic group called a heme group (shown in gray) with a bound oxygen molecule (red). Proteins are large biomolecules and ...
Protein efficiency ratio. Protein efficiency ratio (PER) is based on the weight gain of a test subject divided by its intake of a particular food protein during the test period. From 1919 until very recently [when?], the PER had been a widely used method for evaluating the quality of protein in food.
