Sandbox Reserved 1383

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== 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 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.
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.
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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.
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 ==

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.
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Insulin

Escherichia coli reca protein-bound DNA (PDB entry 3rec)

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