Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins
Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins
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DOI：
10.1021/ja010002z
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发表时间：
2001-06-27
影响因子：
15
通讯作者：
Brüschweiler, R
中科院分区：
文献类型：
--
作者：
Meiler, J;Prompers, JJ;Brüschweiler, R
利用10 ns泛素分子动力学(MD)计算机模拟泛素，分析了液晶环境中部分排列的蛋白质的内部运动对剩余偶极核磁共振偶极耦合的影响。对于一组具有不同取向和菱形的排列张量，确定了MD平均偶极耦合，并随后根据有效排列张量、偶极矢量的平均取向和分子内重定向矢量分布来解释不同情况下的偶极耦合。推导了反映偶极耦合运动标度和偶极驰豫数据标度(核磁共振序参数)之间异同的解析关系式。将本文提出的自洽方法应用于在不同液晶介质中排列的生物分子的偶极耦合测量，应该允许以一种“无模型”的方式提取偶极矢量的平均取向及其运动的特定方面。
The effects of internal motions on residual dipolar NMR couplings of proteins partially aligned in a liquid-crystalline environment are analyzed using a 10 ns molecular dynamics (MD) computer simulation of ubiquitin, For a set of alignment tensors with different orientations and rhombicities, MD-averaged dipolar couplings are determined and subsequently interpreted for different scenarios in terms of effective alignment tensors, average orientations of dipolar vectors, and intramolecular reorientational vector distributions. Analytical relationships are derived that reflect similarities and differences between motional scaling of dipolar couplings and scaling of dipolar relaxation data (NMR order parameters). Application of the self-consistent procedure presented here to dipolar coupling measurements of biomolecules aligned in different liquid-crystalline media should allow one to extract in a "model-free" way average orientations of dipolar vectors and specific aspects of their motions.