Dynamics of insulin probed by 1H-NMR amide proton exchange anomalous flexibility of the receptor-binding surface
Dynamics of Insulin Probed by 1H-NMR Amide Proton E Anomalous Flexibility of the Receptor-Binding Surfa
THIS STRUCTURE WAS DETERMINED USING STANDARD 2D HOMONUCLEAR NMR TECHNIQUES.
RMSD VALUES FOR ALL 20 STRUCTURES VERSUS GEOMETRIC AVERAGE: (BACKBONE, A2-A19, B3-B26) 0.21 ANGSTR
0.5 mM INSULIN A CHAIN-1, 0.5 mM INSULIN B CHAIN-2, 90% H2O/10% D2O
HORMONE, INSULIN, MUTANT, Carbohydrate metabolism, Cleavage on pair of basic residues, Diabetes mellitus, Disease mutation, Disulfide bond, Glucose metabolism, Pharmaceutical, Secreted