Université Grenoble Alpes, Inria, CNRS, Laboratoire Jean Kuntzmann, 38000, Grenoble, France.
J Comput Aided Mol Des. 2019 Aug;33(8):705-727. doi: 10.1007/s10822-019-00216-w. Epub 2019 Aug 21.
The possible functions of a protein are strongly related to its structural rearrangements in the presence of other molecules or environmental changes. Hence, the evaluation of transition paths of proteins, which encodes conformational changes between stable states, is important since it may reveal the underlying mechanisms of the biochemical processes related to these motions. During the last few decades, different geometry-based methods have been proposed to predict such transition paths. However, in the cases where the solution requires complex motions, these methods, which typically constrain only locally the molecular structures, could produce physically irrelevant solutions involving self-intersection. Recently, we have proposed ART-RRT, an efficient method for finding ligand-unbinding pathways. It relies on the exploration of energy valleys in low-dimensional spaces, taking advantage of some mechanisms inspired from computer graphics to ensure the consistency of molecular structures. This article extends ART-RRT to the problem of finding probable conformational transition between two stable states for proteins. It relies on a bidirectional exploration rooted on the two end states and introduces an original strategy to attempt connections between the explored regions. The resulting method is able to produce at low computational cost biologically realistic paths free from self-intersection. These paths can serve as valuable input to other advanced methods for the study of proteins. A better understanding of conformational changes of proteins is important since it may reveal the underlying mechanisms of the biochemical processes related to such motions. Recently, the ART-RRT method has been introduced for finding ligand-unbinding pathways. This article presents an adaptation of the method for finding probable conformational transition between two stable states of a protein. The method is not only computationally cost-effective but also able to produce biologically realistic paths which are free from self-intersection.
蛋白质的可能功能与其在其他分子或环境变化存在下的结构重排密切相关。因此,评估蛋白质的转变路径(编码稳定状态之间的构象变化)非常重要,因为它可能揭示与这些运动相关的生化过程的潜在机制。在过去的几十年中,已经提出了许多基于几何形状的方法来预测这些转变路径。然而,在需要复杂运动的情况下,这些方法通常仅局部限制分子结构,可能会产生涉及自交的物理上无关的解。最近,我们提出了 ART-RRT,这是一种用于寻找配体解吸途径的有效方法。它依赖于在低维空间中探索能量谷,利用一些受计算机图形启发的机制来确保分子结构的一致性。本文将 ART-RRT 扩展到寻找蛋白质两个稳定状态之间可能的构象转变的问题。它依赖于基于两个末端状态的双向探索,并引入了一种原始策略来尝试连接已探索区域之间的连接。所得到的方法能够以较低的计算成本生成没有自交的生物现实路径。这些路径可以作为研究蛋白质的其他高级方法的有价值的输入。更好地了解蛋白质的构象变化很重要,因为它可能揭示与这些运动相关的生化过程的潜在机制。最近,ART-RRT 方法已被引入用于寻找配体解吸途径。本文提出了一种将该方法用于寻找蛋白质两个稳定状态之间可能的构象转变的方法。该方法不仅计算成本效益高,而且能够生成没有自交的生物现实路径。