Sequence-specific 1H-NMR assignments in rabbit-liver metallothionein-2.
Sequence-specific 1H-NMR assignments in rabbit-liver metallothionein-2.
复制标题
兔肝金属硫蛋白-2 中序列特异性 1H-NMR 归属。
DOI：
10.1111/j.1432-1033.1986.tb09666.x
复制
发表时间：
1986
期刊：
影响因子：
--
通讯作者：
K. Wüthrich
中科院分区：
文献类型：
--
作者：
G. Wagner;D. Neuhaus;E. Wörgötter;M. Vašák;J. Kägi;K. Wüthrich
完整的序列特异性分配的1H核磁共振谱的主要亚型兔肝金属硫蛋白-2提出。顺序分配程序揭示了许多不同的结果，关于早期的部分化学测序，现在已知的制剂是微异质。特别是，目前的数据表明，与所有其他已知的哺乳动物金属硫蛋白的61个氨基酸相比，多肽链长度为62个氨基酸残基。在新序列中，通过化学方法也得到了充分的证实，附加的氨基酸残基被鉴定为插入在标准氨基酸编号的Ala8和Ala9之间的Ala8'。除了主要的蛋白质种类外，所有的制备都含有一种次要的成分，其二维1h -核磁共振特征与化学上不同的同源金属硫蛋白兼容。
The complete sequence-specific assignment of the 1H nuclear magnetic resonance spectrum of a major subform of rabbit liver metallothionein-2 is presented. The sequential assignment procedures revealed a number of differences with regard to results obtained by earlier partial chemical sequencing of a preparation now known to be microheterogeneous. In particular, the present data indicate a polypeptide chain length of 62 amino acid residues as compared to the occurrence of 61 amino acids in all other known mammalian metallothioneins. In the new sequence, which was also fully confirmed by chemical means, the additional amino acid residue was identified as Ala8' inserted between Ala8 and Ala9 of the standard amino acid numeration. In addition to the predominant protein species all preparations contained a minor component, for which the two-dimensional 1H-nuclear magnetic resonance features are compatible with a chemically different, homologous metallothionein.
镉、锌金属硫蛋白的单晶。
DOI：
--
发表时间：
1983
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Melis,KA;Carter,DC;Stout,CD;Winge,DR
通讯作者：
Winge,DR