Structural origin of the high affinity of a chemically evolved lanthanide-binding peptide
Structural origin of the high affinity of a chemically evolved lanthanide-binding peptide
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DOI：
10.1002/anie.200460028
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发表时间：
2004-01-01
影响因子：
16.6
通讯作者：
Imperiali, B
中科院分区：
文献类型：
--
作者：
Nitz, M;Sherawat, M;Imperiali, B
用铽玩标签：在与 Tb 3+ 离子复合的化学进化的 17 残基镧系元素结合肽的 2.0-Å 分辨率 X 射线晶体结构中揭示了新的疏水接触和连接氨基酸（参见带状图）。晶体结构与溶液中的发光寿命测量结果非常吻合，这表明复合物中不存在第一壳层配位水分子。
Playing tag with terbium: New hydrophobic contacts and ligating amino acids are revealed in the 2.0-Å resolution X-ray crystal structure of a chemically evolved 17-residue lanthanide-binding peptide complexed with a Tb 3+ ion (see ribbon diagram). The crystal structure agrees well with luminescence-lifetime measurements in solution, which indicate that no first-shell-coordinating water molecules are present in the complex.