Collegen

Collagen

Collagen is a very interesting protein. It is a triple helix and is in a group of naturally occurring proteins that can be found in tendon, ligament and skin, cartilage, bone, blood vessels, the gut, and intervertebral disc of animals. Collagen is the most abundant protein in mammals. It makes up 25% to 35% of the protein in the body, up to 2% of muscle tissue and is 6% of the weight of strong tendinous muscles. When collagen has been hydrolyzed, it becomes gelatin. Collagen is a protein that is rigid and has an approximant molecular weight of 300 kilodaltons and a typical chemical formula ofC2H5NOC5H9NOC5H10NO2. It is roughly 300nm in length and 1.5 nm in diameter. It is a structural protein that creates the physical structure of the body and is the supporting framework that cells are arranged over.

Collagen has a helix for a secondary structure and a triple helix as a tertiary structure. The triple helix is usually composed of two identical chains and a chain that differs only slightly. The two chains that are identical are called 1 and the other similar chain is called 2. These chains are left-handed helix and when twisted together form a right-handed triple helix. This triple helix is held together by hydrogen bonds. Collagen is not a typical protein in its amino acid composition. Collagen is typically made up of glycine and proline or hydroxyproline. The arrangement of these amino acids can be Glycine-Proline-X or Glycine-X- hydroxyproline. The X is for any other amino acid besides glycine, proline or hydroxyproline. These arrangements of amino acids are a distinctive feature of collagen. Glycine accounts for 1/3 of the sequence, while proline or hydroxyproline account for 1/6 of the sequence. This high glycine content is important for the stabilization and is required for every third position so the residue can be put in the center where there is no space for any other residues. The proline, hydroxyproline and other amino...