Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings
Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings
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DOI：
10.1023/a:1026501101716
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发表时间：
2000-11-01
影响因子：
2.7
通讯作者：
Kay, LE
中科院分区：
文献类型：
--
作者：
Skrynnikov, NR;Kay, LE
弱对准液晶溶剂中残余偶极偶联的测量包含了溶液中生物分子结构的宝贵信息。在这里，我们证明了偶极耦合（DCs）可以用来推导出一套不依赖于取向张量主轴方向的全面的成对角约束。这些约束可用于通过称为“DC一致性图”的图形表示来评估试验蛋白质结构和一组实验偶极偶联之间的一致性。重要的是，这些图可以用来识别与实验直流数据一致的结构元素，并确定需要进一步改进的结构参数，这对于基于直流的结构计算的成功至关重要。这种方法适用于42 kDa的麦芽糊精结合蛋白。
Residual dipolar couplings measured in weakly aligning liquid-crystalline solvent contain valuable information on the structure of biomolecules in solution. Here we demonstrate that dipolar couplings (DCs) can be used to derive a comprehensive set of pairwise angular restraints that do not depend on the orientation of the alignment tensor principal axes. These restraints can be used to assess the agreement between a trial protein structure and a set of experimental dipolar couplings by means of a graphic representation termed a 'DC consistency map'. Importantly, these maps can be used to recognize structural elements consistent with the experimental DC data and to identify structural parameters that require further refinement, which could prove important for the success of DC-based structure calculations. This approach is illustrated for the 42 kDa maltodextrin-binding protein.