Insulin Structure & Function: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| Line 6: | 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. | ||
==3D structures of insulin== | |||
[[Insulin]] | |||
==Additional Resources== | ==Additional Resources== | ||
For additional information, see: [[Diabetes & Hypoglycemia]] | For additional information, see: [[Diabetes & Hypoglycemia]] | ||
<br /> | <br /> | ||
