Insulin Structure & Function

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
{{STRUCTURE_2hiu | PDB=2hiu | SCENE= }}
 
- 
<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==
Line 8: Line 6:
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.
-
 
+
</StructureSection>
==3D structures of insulin==
==3D structures of insulin==

Revision as of 02:09, 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

For additional information, see: Diabetes & Hypoglycemia

Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor, Michal Harel, David Canner, Pat McQuaid

Personal tools