HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
HYDRONMR: Prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations
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DOI：
10.1006/jmre.2000.2170
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发表时间：
2000-11-01
影响因子：
2.2
通讯作者：
Carrasco, B
中科院分区：
文献类型：
--
作者：
de la Torre, JG;Huertas, ML;Carrasco, B
球状蛋白质的异核核磁共振弛豫依赖于各向异性的旋转扩散张量。利用我们以前对任意形状颗粒流体动力学性质的预测，通过珠子模型，我们构造了一个计算程序，可以从蛋白质详细的原子级结构计算其旋转扩散张量和其他性质。从用于建立珠模型的原子坐标文件中，可以提取相关偶极子的取向，并结合流体动力学信息来预测蛋白质中的每个残基的驰豫时间。所有这些进展都已在一个名为HYDRO核磁共振的计算机程序中实现，该程序将是公共领域的。(C)2000年学术出版社。
The heteronuclear NMR relaxation of globular proteins depends on the anisotropic rotational diffusion tensor. Using our previous developments for prediction of hydrodynamic properties of arbitrarily shaped particles, by means of bead models, we have constructed a computational procedure to calculate the rotational diffusion tensor and other properties of proteins from their detailed, atomic-level structure. From the atomic coordinates file used to build the bead model, the orientation of the pertinent dipoles can be extracted and combined with the hydrodynamic information to predict, for each residue in the protein, the relaxation times. All of these developments have been implemented in a computer program, HYDRONMR, which will be of public domain. (C) 2000 Academic Press.