Amadei A, Ceruso M A, Di Nola A
Department of Chemistry, University of Rome "La Sapienza," Rome, Italy.
Proteins. 1999 Sep 1;36(4):419-24.
In this article we present a quantitative evaluation of the convergence of the conformational coordinates of proteins, obtained by the Essential Dynamics method. Using a detailed analysis of long molecular dynamics trajectories in combination with a statistical assessment of the significance of the measured convergence, we obtained that simulations of a few hundreds of picoseconds are in general sufficient to provide a stable and statistically reliable definition of the essential and near constraints subspaces, at least within the nanoseconds time range. Proteins 1999;36:419-424.
在本文中，我们对通过主成分动力学方法获得的蛋白质构象坐标收敛情况进行了定量评估。通过对长分子动力学轨迹的详细分析，并结合对所测收敛显著性的统计评估，我们发现，至少在纳秒时间范围内，几百皮秒的模拟通常足以提供对主成分和近约束子空间的稳定且统计可靠的定义。《蛋白质》1999年；第36卷：419 - 424页。
