Ghose R, Huang K, Prestegard J H
Department of Chemistry, Yale University, New Haven, Connecticut, 06520, USA.
J Magn Reson. 1998 Dec;135(2):487-99. doi: 10.1006/jmre.1998.1602.
We present a simple method for extracting interference effects between chemical shift anisotropy (CSA) and dipolar coupling from spin relaxation measurements in macromolecules, and we apply this method to extracting cross-correlation rates involving interference of amide 15N CSA and 15N-1H dipolar coupling and interference of carbonyl 13C' CSA and 15N-13C' dipolar coupling, in a small protein. A theoretical basis for the interpretation of these rates is presented. While it proves difficult to quantitatively separate the structural and dynamic contributions to these cross-correlation rates in the presence of anisotropic overall tumbling and a nonaxially symmetric chemical shift tensor, some useful qualitative correlations of data with protein structure can be seen when simplifying assumptions are made.
我们提出了一种从大分子的自旋弛豫测量中提取化学位移各向异性（CSA）和偶极耦合之间干扰效应的简单方法，并将该方法应用于提取涉及酰胺(^{15}N) CSA与(^{15}N - ^{1}H)偶极耦合干扰以及羰基(^{13}C') CSA与(^{15}N - ^{13}C')偶极耦合干扰的交叉相关速率，该测量针对一种小蛋白质进行。文中给出了这些速率解释的理论基础。虽然在存在各向异性整体翻滚和非轴对称化学位移张量的情况下，定量分离这些交叉相关速率的结构和动力学贡献证明是困难的，但在做出简化假设时，可以看到一些数据与蛋白质结构的有用定性关联。
