通过溶液中的核磁共振研究金属硫蛋白-2两个金属簇中的多肽折叠。
Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution.
作者信息
Braun W, Wagner G, Wörgötter E, Vasák M, Kägi J H, Wüthrich K
出版信息
J Mol Biol. 1986 Jan 5;187(1):125-9. doi: 10.1016/0022-2836(86)90412-2.
PMID:3959078
Abstract
The solution conformation of rabbit liver Cd27+-metallothionein-2 was determined by nuclear magnetic resonance (n.m.r.) and distance geometry. The n.m.r. data are based on complete sequence-specific resonance assignments for the polypeptide chain. This letter describes the global arrangement of the polypeptide chain, which forms two distinct domains containing metal clusters of three and four Cd ions, respectively.
摘要
通过核磁共振（n.m.r.）和距离几何方法确定了兔肝Cd27 + -金属硫蛋白-2的溶液构象。n.m.r.数据基于多肽链完整的序列特异性共振归属。本文描述了多肽链的整体排列，其形成了两个不同的结构域，分别包含三个和四个镉离子的金属簇。
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