Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.
Closed form of liganded glutamine-binding protein by rotational-echo double-resonance NMR.
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DOI：
10.1021/bi9705016
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发表时间：
1997-08
期刊：
影响因子：
2.9
通讯作者：
C. Klug;K. Tasaki;N. Tjandra;C. Ho;J. Schaefer
中科院分区：
文献类型：
--
作者：
C. Klug;K. Tasaki;N. Tjandra;C. Ho;J. Schaefer
旋转回波双共振NMR已被用来确定谷氨酰胺结合蛋白及其配体L-谷氨酰胺复合物的核间距。配体和Tyr 185之间的距离与分子动力学模拟的结果一致，所述分子动力学模拟由三个REDOR确定的到His 156的距离约束。该模型也与其他六个REDOR确定的核间距，其中大部分同意从第一次报告的谷氨酰胺结合蛋白和L-谷氨酰胺的复合物的X射线结构的值是一致的。
Rotational-echo double-resonance NMR has been used to determine internuclear distances in the complex of glutamine-binding protein and its ligand, l-glutamine. The distances between the ligand and Tyr185 are consistent with the results of molecular dynamics simulations constrained by three REDOR-determined distances to His156. This model is also consistent with six other REDOR-determined internuclear distances, most of which agree with values from the first report of an X-ray structure of the complex of glutamine-binding protein and l-glutamine.