环状γ-域类似物（小麦金属硫蛋白 E(c)-1）的溶液结构。

Institute of Inorganic Chemistry, University of Zurich, Winterthurerstrasse 190, Zurich CH-8057, Switzerland.

Molecules. 2013 Nov 21;18(11):14414-29. doi: 10.3390/molecules181114414.

The first cyclic analog of a metallothionein (MT) was prepared and analyzed by UV and (magnetic) circular dichroism spectroscopy, ESI-MS as well as NMR spectroscopy. Results reveal that the evaluated cyclic γ-E(c)-1 domain of the wheat MT E(c)-1 retains its ability to coordinate two Zn(II) or Cd(II) ions and adopts a three-dimensional structure that is highly similar to the one of the linear wild-type form. However, the reduced flexibility of the protein backbone facilitates structure solution significantly and results in a certain stabilization of metal binding to the protein.

一种金属硫蛋白（MT）的首个环状类似物已通过紫外和（圆二色性）光谱、电喷雾质谱以及核磁共振波谱进行了制备和分析。结果表明，评估的小麦 MT E(c)-1 的环状 γ-E(c)-1 结构域保留了与两个 Zn(II)或 Cd(II)离子配位的能力，并采用了与线性野生型形式高度相似的三维结构。然而，蛋白质主链的柔韧性降低显著促进了结构解析，并导致金属与蛋白质结合的一定稳定性。