Insulin Structure & Function: Difference between revisions

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==Structure==
==Structure==


Insulin is composed of two different types of peptide chains. <scene name='34/347648/Chain_a/1'>Chain A</scene> has 21 amino acids and <scene name='34/347648/Chain_b/1'>Chain B</scene> has 30 amino acids.  Both chains contain <scene name='34/347648/Secondary_structures/1'>alpha helices</scene> but no beta strands. There are 3 conserved <scene name='34/347648/Disulfide_bonds/1'>disulfide bridges</scene> which help keep the two chains together.  Insulin can also form <scene name='User:Whitney_Stoppel/sandbox1/Insulin_dimer/2'>dimers</scene> in solution due to the hydrogen bonding between the B chains (shown as white lines).  The dimers can further interact to form <scene name='User:Whitney_Stoppel/sandbox1/Insulin_hexamer/4'>hexamers</scene> due to interaction between hydrophobic surfaces.  This <scene name='User:Whitney_Stoppel/sandbox1/Insulin_ph7/2'>scene highlights</scene> the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.  Indeed "fast acting" insulin is produced by switching the last two amino acids, which reduces the formation of the hexameric insulin.
Insulin is composed of two different types of peptide chains. <scene name='34/347648/Chain_a/1'>Chain A</scene> has 21 amino acids and <scene name='34/347648/Chain_b/1'>Chain B</scene> has 30 amino acids.  Both chains contain <scene name='34/347648/Secondary_structures/1'>alpha helices</scene> but no beta strands. There are 3 conserved <scene name='34/347648/Disulfide_bonds/1'>disulfide bridges</scene> which help keep the two chains together.  Insulin can also form <scene name='User:Whitney_Stoppel/sandbox1/Insulin_dimer/2'>dimers</scene> in solution due to the hydrogen bonding between the B chains (shown as white lines).  The dimers can further interact to form <scene name='User:Whitney_Stoppel/sandbox1/Insulin_hexamer/4'>hexamers</scene> due to interaction between hydrophobic surfaces.  This <scene name='User:Whitney_Stoppel/sandbox1/Insulin_ph7/2'>scene highlights</scene> the hydrophobic (gray) and polar (purple) parts of an insulin monomer at a pH of 7.   
 
A number of insulin variants have been made to favor either the monomeric or hexameric form.  Deletion of the <scene name='34/347648/Hexamer_bchaincterminus/2'>five C terminal residues of the B chain</scene> creates a monomer only form.  This portion of the B chain is involved in <scene name='34/347648/Dimer_bchainctermhbond/1'>hydrogen bonds</scene> between the B chain of one monomer and the A (marked C) and B (marked D) chain of another monomer.
 
</StructureSection>
</StructureSection>
==3D structures of insulin==
==3D structures of insulin==

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Pat McQuaid, Student, David Canner, Michal Harel, Ann Taylor