NMR STRUCTURE OF HUMAN INSULIN MUTANT ILE-A2-ALA, HIS-B10-ASP, PRO-B28-LYS, LYS-B29-PRO, 15 STRUCTURES
A cavity-forming mutation in insulin induces segmental unfolding of a surrounding alpha-helix.
The peptide was chemically synthesized. The sequence of the peptide is naturally found in Homo sapiens (human).
This structure was determined using standard 2D homonuclear techniques.
The structure is based on a total of 416 restraints, 367 are NOE-derived distance constraints, 32 dihedral angle restraints, 17 distance restraints from hydrogen bonds.
distance geometry and simulated annealing
1.2 mM AlaA2-DKP-Insulin; 90% H2O, 10% D2O;
1.2 mM AlaA2-DKP-Insulin; 20% Deuteroacetic Acid, 80% D2O;
HORMONE, HUMAN INSULIN, MUTANT, HORMONE-GROWTH FACTOR COMPLEX