Comparison of the 13C relaxation times and proton scalar couplings of BPTI with values predicted by molecular dynamics.
Comparison of the 13C relaxation times and proton scalar couplings of BPTI with values predicted by molecular dynamics.
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DOI：
10.1006/jmrb.1994.1081
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发表时间：
1994-07
期刊：
影响因子：
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通讯作者：
S. Balasubramanian;R. Nirmala;D. Beveridge;P. Bolton
中科院分区：
文献类型：
--
作者：
S. Balasubramanian;R. Nirmala;D. Beveridge;P. Bolton
将实验测得的~(13)C驰豫时间与分子动力学模拟的预测值进行了比较。由于碳-13T1值是蛋白质内部运动速度和幅度的灵敏监测器，所以进行这种比较是为了测试分子动力学在多大程度上提供了蛋白质内部运动的准确描述。还比较了实验和预测的酰胺-α标量偶联，因为这种偶联依赖于蛋白质的构象。这些比较表明，分子动力学模拟预测的结果与实验数据总体上是一致的。
The experimental carbon-13 relaxation times of BPTI have been compared with the values predicted by molecular-dynamics simulations. Since the carbon-13 T1 values are sensitive monitors of the rates and amplitudes of the internal motions of the protein, this comparison was made to test the extent to which molecular dynamics provides an accurate depiction of the internal motions of proteins. The experimental and predicted amide-alpha scalar couplings were also compared, since this coupling is dependent on the conformation of the protein. These comparisons have shown that the molecular-dynamics simulation predicts results that are in good overall agreement with the experimental data.