Tolman Joel R
Institut de Chimie Moléculaire et Biologique, Ecole Polytechnique Fédérale de Lausanne BCH, 1015 Lausanne, Switzerland.
J Am Chem Soc. 2002 Oct 9;124(40):12020-30. doi: 10.1021/ja0261123.
The interpretation of residual dipolar couplings in terms of molecular properties of interest is complicated because of difficulties in separating structural and dynamic effects as well as the need to estimate alignment tensor parameters a priori. An approach is introduced here that allows many of these difficulties to be circumvented when data are acquired in multiple alignment media. The method allows the simultaneous extraction of both structural and dynamic information directly from the residual dipolar coupling data, in favorable cases even in the complete absence of prior structural knowledge. Application to the protein ubiquitin indicates greater amplitudes of internal motion than expected from traditional (15)N spin relaxation analysis.
由于难以区分结构和动力学效应以及需要先验估计取向张量参数，根据感兴趣的分子特性来解释剩余偶极耦合变得很复杂。本文介绍了一种方法，当在多种取向介质中获取数据时，可以规避许多此类困难。该方法允许直接从剩余偶极耦合数据中同时提取结构和动力学信息，在有利的情况下，甚至在完全没有先验结构知识的情况下也能做到。应用于蛋白质泛素表明，其内部运动幅度比传统的（15）N自旋弛豫分析预期的要大。
