Structural modifications of oxidized insulin B-chain induced by glycerol addition

Abstract

1H-NMR studies of the bovine insulin S-sulfonated B-chain are reported in H20/D2 O (9/1) and in glycerol-d5 (5 M) using two-dimensional NMR spectroscopy. The first results show that the oxidized insulin B-chain secondary structure differs from that of native insulin by a loss of the a-helix between the two disulfide bridges and that the glycerol favours the structuring of the peptide.