Single-molecule force spectroscopy and classical molecular dynamics are natural allies. Recent advances in both experiments and simulations have increasingly facilitated a direct comparison of SMFS and MD data, most importantly by closing the gap between time scales, which has been traditionally at least 5 orders of magnitudes wide. In this review, we will explore these advances chiefly on the computational side. We focus on protein dynamics under force and highlight recent studies that showcase how lower loading rates and more statistics help to better interpret previous experiments and to also motivate new ones. At the same time, steadily increasing system sizes are used to mimic more closely the mechanical environment in the biological context. We showcase some of these advances on atomistic and coarse-grained scale, from asymmetric membrane tension to larger (multidomain/multimeric) protein assemblies under force.

中文翻译：

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蛋白质机械性质和功能的分子模拟研究进展。

单分子力谱和经典分子动力学是自然的盟友。实验和仿真方面的最新进展日益促进了对SMFS和MD数据的直接比较，最重要的是通过缩小了时标之间的间隔，该时标通常至少为5个数量级。在这篇综述中，我们将主要在计算方面探索这些进展。我们专注于受力的蛋白质动力学，并着重强调最近的研究，这些研究展示了较低的上样率和更多的统计数据如何帮助更好地解释以前的实验并激发新的实验。同时，稳步增加的系统尺寸用于在生物学环境中更紧密地模拟机械环境。我们以原子和粗粒度展示了其中的一些进步，