Protein backbone 15N relaxation rates as a tool for the diagnosis of structure quality
Protein backbone 15N relaxation rates as a tool for the diagnosis of structure quality
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DOI：
10.1006/jmre.2000.2063
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发表时间：
2000-06-01
影响因子：
2.2
通讯作者：
Tjandra, N
中科院分区：
文献类型：
--
作者：
de Alba, E;Tjandra, N
在本文报道的工作中，我们定义了一个依赖于蛋白质骨架N-15弛豫速率的结构验证因子。这是一种替代方法，以前定义的品质因子来自各向异性化学位移或残留偶极耦合。我们已经使用了N-15各向异性翻滚蛋白质的弛豫速率的结构依赖性来计算这个结构诊断因子，并用它来证明改进的蛋白质结构与残余偶极耦合精制。
In the work reported herein we define a structure validation factor that depends on protein backbone N-15 relaxation rates. This is an alternative method to the previously defined quality factors derived from anisotropic chemical shifts or residual dipolar couplings. We have used the structure dependence of N-15 relaxation rates of anisotropically tumbling proteins to calculate this structure diagnosis factor and have used it to demonstrate the improvement of protein structures refined with residual dipolar couplings.