Crystal structure of an unstable insulin analog with native activity.
Non-standard insulin design: structure-activity relationships at the periphery of the insulin receptor.
Diabetes-associated mutations in a beta-cell transcription factor destabilize an antiparallel "mini-zipper" in a dimerization interface
The Relationship Between Insulin Bioactivity and Structure in the NH2-terminal A-chain Helix
Mapping the Functional Surface of Insulin by Design: Structure and Function of a Novel A-chain Analogue
A Proposed Interaction Model of the Insulin Molecule with its Receptor
Tris, phonel, acetone, sodium citrate, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 298K
1TRZ contains the same sequence and structure, without substitution of Thr-A8 by diaminobutyric acid
COMPOUND THE CONFORMATIONS OF TWO MONOMERS ARE DIFFERENT AS THE RESULT OF A CHANGE IN CONFORMATION OF THE FIRST EIGHT RESIDUES OF THE B-CHAINS.
The protein was chemically synthesized. The sequence is naturally found in Homo sapiens(human).
A8-Diaminobutyric Acid human insulin, hormone-receptor interface, HORMONE-GROWTH FACTOR COMPLEX