What is the structure of insulin and how is it activated from its precursor form?
Insulin is a small peptide hormone with 51 amino acids, consisting of two polypeptide chains linked by disulfide bonds. It is initially secreted as proinsulin, an inactive zymogen, by pancreatic beta cells. Proinsulin is activated through proteolysis, which removes a connecting segment and results in the active, two-chain insulin molecule.