Insulin Structure & Function
From Proteopedia
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<StructureSection load='' size='500' side='right' scene='2hiu' caption='Human insulin chain A (grey) and chain B (green), [[2hiu]]'> | <StructureSection load='' size='500' side='right' scene='2hiu' caption='Human insulin chain A (grey) and chain B (green), [[2hiu]]'> | ||
==Function== | ==Function== | ||
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Insulin is monomeric and is composed of two polypeptide chains. It is composed of two different types of peptide chains. Chain A has 21 amino acids and Chain B has 30 amino acids. Insulin has a three dimensional structure consisting of 3 helices and 3 conserved disulfide bridges. The molecules in insulin sometimes form dimers in solution due to the hydrogen bonding between the B chains. Granules consisting hexamers are also sometimes formed by insulin. This is caused by the intercation between hydrophobic surfaces. | Insulin is monomeric and is composed of two polypeptide chains. It is composed of two different types of peptide chains. Chain A has 21 amino acids and Chain B has 30 amino acids. Insulin has a three dimensional structure consisting of 3 helices and 3 conserved disulfide bridges. The molecules in insulin sometimes form dimers in solution due to the hydrogen bonding between the B chains. Granules consisting hexamers are also sometimes formed by insulin. This is caused by the intercation between hydrophobic surfaces. | ||
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==3D structures of insulin== | ==3D structures of insulin== | ||
Revision as of 02:09, 26 March 2015
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3D structures of insulin
Additional Resources
For additional information, see: Diabetes & Hypoglycemia