利用质子核磁共振光谱法研究金属硫蛋白的结构。

Investigation of the structure of metallothioneins by proton nuclear magnetic resonance spectroscopy.

作者信息

Vasák M, Galdes A, Hill H A, Kägi J H, Bremner I, Young B W

出版信息

Biochemistry. 1980 Feb 5;19(3):416-25. doi: 10.1021/bi00544a003.

Abstract

The proton nuclear magnetic resonance spectra of metallothioneins from horse, human, and sheep livers were investigated. The spectra of the metallothioneins from the three species are similar as are the two isoproteins from any one species. The spectra indicate that metallothioneins possess a well-defined tertiary structure. Zinc(II) and calcium(II) ions induce similar but not identical tertiary structures. Confirmatory evidence was obtained for the involvement of cysteine residues in metal binding, but no evidence was obtained for the involvement of any other amino acid residue in metal binding. The apoprotein thionein was found to exist essentially in a random-coil conformation with perhaps some residual segmental structure.

摘要

对来自马、人和羊肝脏的金属硫蛋白的质子核磁共振谱进行了研究。这三个物种的金属硫蛋白谱相似，任何一个物种的两种同型蛋白的谱也相似。这些谱表明金属硫蛋白具有明确的三级结构。锌（II）和钙（II）离子诱导相似但不完全相同的三级结构。获得了半胱氨酸残基参与金属结合的确证，但未获得其他任何氨基酸残基参与金属结合的证据。发现脱辅基蛋白硫蛋白基本上以无规卷曲构象存在，可能带有一些残余的片段结构。