Sandbox-insulin-shelly
Insulin is a hormone that controls carbohydrate metabolism and storage in the human body. The body is able to sense the concentration of glucose in the blood and respond by secreting insulin, which is produced by beta cells in the pancreas. Synthesis of human insulin in E. coli is important to producing insulin for the treatment of type 1 diabetes. Proinsulin (Pins) is processed by several proteases in the Golgi apparatus to form insulin which is shorter by 35 amino acids. DPI is a monomeric despentapeptide (B26-B30) Ins analogue. DTRI is a monomeric destripeptide (B28-B30) Ins analogue. DHPI is for desheptapeptide (B24-B30) Ins. LIns is a legume Ins. Insulin is composed of two different types of peptide chains. has 21 amino acids and has 30 amino acids. Both chains contain but no beta strands. There are 3 conserved which help keep the two chains together. Insulin can also form in solution due to the hydrogen bonding between the B chains (shown as white lines). The dimers can further interact to form due to interaction between hydrophobic surfaces. This the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7. Insulin is able to pair-up with itself and form a dimer by forming hydrogen bonds between the ends of two B-chains. These are shown above in white. Then, 3 dimers can come together in the presence of zinc ions and form a hexamer. Insulin is stored in the in the body. This the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7. It is believed that the hydrophobic sections on the B-chain cause insulin aggregation which initially caused problems in the manufacture and storage of insulin for pharmaceutical use. |
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For additional details see Insulin Structure & Function.