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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.
Ionization and Brønsted character of N-terminal amino, C-terminal carboxylate, and side chains of amino acid residues The common natural forms of amino acids have a zwitterionic structure, with −NH + 3 (−NH + 2 − in the case of proline) and −CO − 2 functional groups attached to the same C atom, and are thus α-amino acids, and are the only ones found in proteins during translation ...
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.
Metformin, sold under the brand name Glucophage, among others, is the main first-line medication for the treatment of type 2 diabetes,[12][13][14][15] particularly in people who are overweight.[13] It is also used in the treatment of polycystic ovary syndrome.[14] It is sometimes used as an off-label adjunct to lessen the risk of metabolic ...
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.