Insulin Structure & Function: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Ann Taylor (talk | contribs)
No edit summary
Ann Taylor (talk | contribs)
No edit summary
Line 5: Line 5:
==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
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.
</StructureSection>
</StructureSection>
==3D structures of insulin==
==3D structures of insulin==

Revision as of 03:59, 26 March 2015

Human insulin chain A (grey) and chain B (green), 2hiu

Drag the structure with the mouse to rotate

3D structures of insulin

Insulin

Additional Resources

Thanks to 'User:Whitney_Stoppel' for the hexameric insulin scenes. For additional information, see: Diabetes & Hypoglycemia

Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor, Pat McQuaid, David Canner, Michal Harel