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Insulin Insulin: the protein of the 20th century • One of the first proteins crystallized in 1926 (Structural Genomics) • First protein fully sequenced in 1955 (Bioinformatics) • First protein chemically synthesized in 1958 • First human protein manufactured via recombinant in 1979 (Biotechnology) Studying the three-dimensional structure of insulin As described above, human insulin consists of 51 amino acids, divided into two chains, commonly labeled A and B, with 21 and 30 amino acids respectively. The chains are linked by three disulfide bridges, two forming inter-chain cystine at A7-B7 and A20-B19, and one forming an intra-chain cystine at A6-A11. A piece of anti-parallel b-sheet is formed upon dimerization: residues B23 to B28 of one monomer lie anti-parallel to the same stretch in the other monomer. There are two very small a-helices in the A chain, and a three turn a-helix running from residues B9 to B19 is found in every insulin structure known so far.