A helical conformation of a polypeptide chain, usually right-handed, with maximal intrachain hydrogen bonding; one of the most common secondary structures in proteins.
Intein is an intervening polypeptide which can catalytic self-cleavage from a pre-protein accompanied by the concomitant joining of the two flanking polypeptides (the extein) through a peptide bond.
Now, along with insulin, beta cells also secrete islet amyloid polypeptide, or amylin, so while beta cells are cranking out insulin they also secrete an increased amount of amylin.
Likewise if we were to take this simple polypeptide as all these amino acids come out and just look at the covalent bonds, it doesn't give us that structure of that overall protein.
After it gets a little bit down on that, the ribosome will attach to the rough E.R. and then it will actually make the protein inside the E.R. So eventually that polypeptide will fold and it'll make a protein.