Sandbox Reserved 1383
From Proteopedia
(Difference between revisions)
| (22 intermediate revisions not shown.) | |||
| Line 10: | Line 10: | ||
Type 2 diabetes is quite different from type 1 diabetes in that insulin is present in the body. The cells insulin receptors become resistant to insulin which means that glucose no longer is taken up and blood sugar levels remain high. This causes beta cells in the pancreas to work harder to produce more and more insulin until they become exhausted to the point that very little insulin is being produced. | Type 2 diabetes is quite different from type 1 diabetes in that insulin is present in the body. The cells insulin receptors become resistant to insulin which means that glucose no longer is taken up and blood sugar levels remain high. This causes beta cells in the pancreas to work harder to produce more and more insulin until they become exhausted to the point that very little insulin is being produced. | ||
== Structural highlights == | == Structural highlights == | ||
| - | Insulin is composed of two polypeptide chains, an A chain and a B chain. The A chain is composed of 21 amino acids while the B chain is 30 amino acids long. They are joined together by disulfide bridges. Both chains contain alpha helices but no beta pleated sheets. Binding of insulin to its insulin receptor is limited to the B chain. | + | Insulin is composed of two polypeptide chains, an A chain and a B chain. The A chain is composed of 21 amino acids while the B chain is 30 amino acids long. They are joined together by 3 <scene name='77/777703/Disulfide_bridges_of_insulin/2'>disulfide bridges</scene>, 2 linking the A and B chains together, and one internally linking the A chain. Both chains contain <scene name='77/777703/Alpha_helices_of_insulin/1'>alpha helices</scene> but no beta pleated sheets. Binding of insulin to its insulin receptor is limited to the B chain. The general tertiary structure of insulin is highly conserved among species, and can be used to treat human deficiencies. Pig insulin is a common substitute for human insulin. |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| + | The <scene name='77/777703/Hydrophobic_regions_of_insulin/1'>hydrophobic regions of insulin</scene> cause the folding of the A and B chains into the protein structure as shown. Hydrogen bonding allows dimers to form between insulin molecules. Insulin molecules naturally form dimers, and do not affect the rate of absorption into a cell. Hexadimers, which are hydrogen bonded complexes between 6 insulin molecules, do slow down the rate of absorption due to its size. | ||
== References == | == References == | ||
https://www.diabetesselfmanagement.com/blog/what-does-insulin-do/ | https://www.diabetesselfmanagement.com/blog/what-does-insulin-do/ | ||
| Line 23: | Line 18: | ||
https://www.rcsb.org/structure/3I40 | https://www.rcsb.org/structure/3I40 | ||
| - | <references/ | + | <references/> |
| - | + | ||
Current revision
| This Sandbox is Reserved from January through July 31, 2018 for use in the course HLSC322: Principles of Genetics and Genomics taught by Genevieve Houston-Ludlam at the University of Maryland, College Park, USA. This reservation includes Sandbox Reserved 1311 through Sandbox Reserved 1430. |
To get started:
More help: Help:Editing |
Insulin
| |||||||||||
