| THE CHARACTERISTICS AND MOTION MODEL OF INSULIN MONOMER |
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| 作者姓名： | 梁栋材 常文瑞 王大成 张季平 |
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| 作者单位： | National Laboratory of Biomacromolecules，Institute of Biophysics，Academia Sinica，Beijing 100080，PRC，National Laboratory of Biomacromolecules，Institute of Biophysics，Academia Sinica，Beijing 100080，PRC，National Laboratory of Biomacromolecules，Institute of Biophysics，Academia Sinica，Beijing 100080，PRC，National Laboratory of Biomacromolecules，Institute of Biophysics，Academia Sinica，Beijing 100080，PRC |
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| 基金项目： | Project supported by Academia Sinica and the National Natural Science Foundation of China. |
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| 摘 要： | The extensive conformational comparisons among the determined structures of the differeat 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 10; the mobility for each residue side-chain was very different due to the different surroundings.
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THE CHARACTERISTICS AND MOTION MODEL OF INSULIN MONOMER |
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| LIANG DONG-CAI CHANG WEN-RUI WANG DA-CHENG AND ZHANG JI-PING.THE CHARACTERISTICS AND MOTION MODEL OF INSULIN MONOMER[J].Science in China(Chemistry),1992(4). |
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| Authors: | LIANG DONG-CAI CHANG WEN-RUI WANG DA-CHENG AND ZHANG JI-PING |
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| Abstract: | The extensive conformational comparisons among the determined structures of the differeat 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 10; the mobility for each residue side-chain was very different due to the different surroundings. |
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| Keywords: | structure and function of insulin structural characteristics of insulin monomer motion model of insulin molecule |
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