Balasubramanian S, Nirmala R, Beveridge D L, Bolton P H
Department of Chemistry, Wesleyan University, Middletown, Connecticut 06459.
J Magn Reson B. 1994 Jul;104(3):240-9. doi: 10.1006/jmrb.1994.1081.
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.
已将抑肽酶的实验性碳-13弛豫时间与分子动力学模拟预测的值进行了比较。由于碳-13 T1值是蛋白质内部运动速率和幅度的灵敏监测指标，因此进行此比较是为了检验分子动力学在多大程度上能准确描述蛋白质的内部运动。还比较了实验性和预测的酰胺-α标量耦合，因为这种耦合取决于蛋白质的构象。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吻合良好。
