一种从碳-13核磁共振弛豫数据分析蛋白质侧链动力学的简单方法。
A simple approach to analyzing protein side-chain dynamics from 13C NMR relaxation data.
作者信息
Daragan V A, Mayo K H
机构信息
Biomedical Engineering Center, 4-225 Millard Hall, University of Minnesota, 435 Delaware St., S.E., Minneapolis, Minnesota 55455, USA.
出版信息
J Magn Reson. 1998 Feb;130(2):329-34. doi: 10.1006/jmre.1997.1310.
A simple approach to deriving motional dynamics information of protein and peptide side chains by using 13C NMR relaxation data is presented. By using linear approximation of internal rotational correlation functions, simple equations for relating side-chain conformation, bond rotational amplitudes, and rotational correlation coefficients with different NMR relaxation parameters have been obtained. Auto- and cross-correlation spectral densities are considered, and it is shown that proton-coupled 13C NMR relaxation measurements allow detailed motional information to be obtained.
本文提出了一种利用¹³C NMR弛豫数据推导蛋白质和肽侧链运动动力学信息的简单方法。通过使用内部旋转相关函数的线性近似，得到了将侧链构象、键旋转幅度和旋转相关系数与不同NMR弛豫参数相关联的简单方程。考虑了自相关和交叉相关谱密度，结果表明质子耦合的¹³C NMR弛豫测量能够获得详细的运动信息。
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