Technical University of Munich, Physics Department and Center of Functional Protein Assemblies, Garching, Germany.
Methods Mol Biol. 2024;2780:289-302. doi: 10.1007/978-1-0716-3985-6_15.
Accurate prediction and evaluation of protein-protein complex structures is of major importance to understand the cellular interactome. Predicted complex structures based on deep learning approaches or traditional docking methods require often structural refinement and rescoring for realistic evaluation. Standard molecular dynamics (MD) simulations are time-consuming and often do not structurally improve docking solutions. Better refinement can be achieved with our recently developed replica-exchange-based scheme employing different levels of repulsive biasing between proteins in each replica simulation (RS-REMD). The bias acts specifically on the intermolecular interactions based on an increase in effective pairwise van der Waals radii without changing interactions within each protein or with the solvent. It allows for an improvement of the predicted protein-protein complex structure and simultaneous realistic free energy scoring of protein-protein complexes. The setup of RS-REMD simulations is described in detail including the application on two examples (all necessary scripts and input files can be obtained from https://gitlab.com/TillCyrill/mmib ).
准确预测和评估蛋白质-蛋白质复合物结构对于理解细胞相互作用组至关重要。基于深度学习方法或传统对接方法预测的复合物结构通常需要进行结构精修和重新评分,以进行实际评估。标准分子动力学 (MD) 模拟既耗时又常常不能在结构上改进对接解决方案。我们最近开发的基于 replica-exchange 的方案可以通过在每个 replica 模拟中对蛋白质之间的相互作用施加不同程度的排斥偏置 (RS-REMD) 来实现更好的精修。该偏置专门作用于基于有效对范德华半径增加的分子间相互作用,而不会改变每个蛋白质内或与溶剂的相互作用。它可以改进预测的蛋白质-蛋白质复合物结构,并同时对蛋白质-蛋白质复合物进行现实的自由能评分。RS-REMD 模拟的设置将详细描述,包括两个示例的应用(所有必要的脚本和输入文件都可以从 https://gitlab.com/TillCyrill/mmib 获得)。