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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.
Structure of a typical L-alpha-amino acid in the "neutral" form Amino acids are organic compounds that contain both amino and carboxylic acid functional groups.[1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins.[2] Only these 22 appear in the genetic code of life.[3 ...
A protein is a polyamide. Secondary structure: regularly repeating local structures stabilized by hydrogen bonds. The most common examples are the α-helix, β-sheet and turns. Because secondary structures are local, many regions of different secondary structure can be present in the same protein molecule.
Escherichia coli (/ ˌ ɛ ʃ ə ˈ r ɪ k i ə ˈ k oʊ l aɪ / ESH-ə-RIK-ee-ə KOH-ly) is a gram-negative, facultative anaerobic, rod-shaped, coliform bacterium of the genus Escherichia that is commonly found in the lower intestine of warm-blooded organisms. Most E. coli strains are harmless, but some serotypes such as EPEC, and ETEC are pathogenic and can cause serious food poisoning in ...
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.
