Statistical analysis of conformational changes of proteins

随着计算机硬件和软件的发展，模拟生物分子的功能相关构象变化成为可能。然而，另一方面，模拟数据量迅速增加，并且在没有统计分析的情况下处理如此大量的数据变得困难。在这项研究中，我们已经开发了一个框架的分子动力学模拟数据的统计分析。所开发的框架被成功地应用于两种情况下的构象变化数据：（i）腺苷酸激酶中最慢的自由度（包括P-环和铰链区）从9微秒的模拟数据中被识别。(ii)自由能差异沿着构象变化的多药物转运蛋白AcrB的途径被成功地评估。

With the help of recent advances in computer hardware and software, it is becoming possible to simulate functionally relevant conformational changes of biomolecules. On the other hand, however, the amount of simulation data is rapidly increasing and it is becoming difficult to treat such large amount of data without statistical analysis. In this study, we have developed a framework for the statistical analysis of molecular dynamics simulation data. The developed framework was successfully applied to conformational change data of two cases: (i) The most slowest degrees of freedom (involving the P-loop and a hinge region) in Adenylate Kinase was identified from 9 microseconds simulation data. (ii) Free energy differences along the conformational change pathways of multidrug transporter AcrB was successfully evaluated.