Hawkins B L, Cross K J, Craik D J
Victorian College of Pharmacy, Monash University, Parkville, Australia.
Biochim Biophys Acta. 1994 Dec 14;1209(2):177-82. doi: 10.1016/0167-4838(94)90182-1.
The 1H-NMR chemical shift assignments for the oxidized A-chain of bovine insulin have been determined in aqueous and 30% trifluoroethanol/water solutions. Analysis of the observed medium-range nuclear Overhauser effects indicates that in aqueous solution significant populations of the peptide exist, with a 3(10)-helical conformation over residues 12-17. This region corresponds to helix A (13-20) in the crystal structure of the 2 Zn insulin hexamer. In 30% TFE solution, the NOE data are supportive of a random coil conformation throughout the peptide.
