title: The characteristics and motion model of insulin monomer.
abstract: The extensive conformational comparisons among the determined structures of the different species and crystal forms of insulin and the varied insulin derivatives were performed by using the least-squares superimposition technique and the graphics technique. The results of the investigation showed that the structure of molecule I in 2Zn insulin was closer to that of the natural monomer; the conformational difference between two molecules of a dimer came out during dimerization and it was further improved and stabilized during the hexamerization and packing of hexamers in crystal; through the hinge peptides, such as A10, B4, B8, B24, B20 and B23, there was a flexible relative motion among the structural segments in the insulin molecule, and the residues at the B-chain C-terminal might have a shift of more than 10A; the mobility for each residue side-chain was very different due to the different surroundings.
authors.affiliation: National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, PRC.
authors.forename: D C
authors.initials: DC
authors.lastname: Liang
authors.forename: W R
authors.initials: WR
authors.lastname: Chang
authors.forename: D C
authors.initials: DC
authors.lastname: Wang
authors.forename: J P
authors.initials: JP
authors.lastname: Zhang
mesh_terms: D007328:Insulin / Q000031:analogs & derivatives / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D015394:Molecular Structure; D013329:Structure-Activity Relationship
chemical_list: D007328:Insulin