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CRYSTAL STRUCTURE DETERMINATION OF DESHEPTAPEPTIDE (B24—B30)-INSULIN
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作者 王大成 陆国光 +4 位作者 张季平 谢殿霖 常文瑞 鲁子贤 梁栋材 《Science China Chemistry》 SCIE EI CAS 1989年第2期155-165,共11页
Desheptapeptide (B24—B30)-insulin (DHPI), an essentially inactive insulin analog, is crystallized in space group P2_12_12_1 with two molecules in an asymmetric unit. The orientations of the molecules in the crystal c... Desheptapeptide (B24—B30)-insulin (DHPI), an essentially inactive insulin analog, is crystallized in space group P2_12_12_1 with two molecules in an asymmetric unit. The orientations of the molecules in the crystal cell have been determined by using Patterson search method at 6 resolution and the positions of the molecules are deduced from translation function calculation and R search at 3. resolution. After using the rigid body refinement (CORELS) further to refine the orientational and positional parameters as well as the initial energy restrained refinement (EREF) for the model, the crystallographic R valueis reduced to 0.384 at 3 resolution. The initial Fourier map shows that the B-chain N-terminal (B1—B8) and C-terminal (B20—B22)segments, compared with the native 2 zinc insulin, exhibit drastic conformational changes, but the three helices of B- and A-chains and their relative arrangement are essentially kept in DHPI. 展开更多
关键词 INSULIN ANALOG desheptapeptide INSULIN x-rayanalysis CRYSTAL structure.
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