https://wiki.tiffa.net/w/index.php?action=history&feed=atom&title=Translations%3AInsulin%2F24%2FenTranslations:Insulin/24/en - Revision history2026-08-25T02:02:21ZRevision history for this page on the wikiMediaWiki 1.43.0https://wiki.tiffa.net/w/index.php?title=Translations:Insulin/24/en&diff=129878&oldid=prevFuzzyBot: Importing a new version from external source2024-03-18T07:33:31Z<p>Importing a new version from external source</p>
<p><b>New page</b></p><div>Contrary to an initial belief that hormones would be generally small chemical molecules, as the first peptide hormone known of its structure, insulin was found to be quite large. A single protein (monomer) of human insulin is composed of 51 [[amino acid]]s, and has a [[molecular mass]] of 5808 [[Dalton (unit)|Da]]. The [[molecular formula]] of human insulin is C<sub>257</sub>H<sub>383</sub>N<sub>65</sub>O<sub>77</sub>S<sub>6</sub>. It is a combination of two peptide chains ([[protein dimer|dimer]]) named an A-chain and a B-chain, which are linked together by two [[disulfide bond]]s. The A-chain is composed of 21 amino acids, while the B-chain consists of 30 residues. The linking (interchain) disulfide bonds are formed at cysteine residues between the positions A7-B7 and A20-B19. There is an additional (intrachain) disulfide bond within the A-chain between cysteine residues at positions A6 and A11. The A-chain exhibits two α-helical regions at A1-A8 and A12-A19 which are antiparallel; while the B chain has a central α -helix (covering residues B9-B19) flanked by the disulfide bond on either sides and two β-sheets (covering B7-B10 and B20-B23).</div>FuzzyBot