Heinrich Julian, Krone Michael, O'Donoghue Seán I, Weiskopf Daniel
VISUS, University of Stuttgart, Germany. {kroneml|weiskopf}@visus.uni-stuttgart.de.
Faraday Discuss. 2014;169:179-93. doi: 10.1039/c3fd00138e. Epub 2014 Jun 12.
Intrinsically disordered regions (IDRs) in proteins are still not well understood, but are increasingly recognised as important in key biological functions, as well as in diseases. IDRs often confound experimental structure determination-however, they are present in many of the available 3D structures, where they exhibit a wide range of conformations, from ill-defined and highly flexible to well-defined upon binding to partner molecules, or upon post-translational modifications. Analysing such large conformational variations across ensembles of 3D structures can be complex and difficult; our goal in this paper is to improve this situation by augmenting traditional approaches (molecular graphics and principal components) with methods from human-computer interaction and information visualisation, especially parallel coordinates. We present a new tool integrating these approaches, and demonstrate how it can dissect ensembles to reveal functional insights into conformational variation and intrinsic disorder.
蛋白质中的内在无序区域（IDR）目前仍未得到充分理解，但它们在关键生物学功能以及疾病中的重要性正日益得到认可。IDR常常使实验性结构测定变得复杂——然而，它们存在于许多现有的三维结构中，在这些结构中，它们呈现出广泛的构象，从不明确且高度灵活到与伴侣分子结合或进行翻译后修饰时变得明确。分析三维结构集合中的这种巨大构象变化可能既复杂又困难；我们在本文中的目标是通过将人机交互和信息可视化方法（特别是平行坐标）与传统方法（分子图形学和主成分分析）相结合来改善这种情况。我们展示了一种整合这些方法的新工具，并演示了它如何剖析结构集合以揭示对构象变化和内在无序的功能洞察。
