Single-molecule force spectroscopy techniques allow for the measurement of several static and dynamic features of macromolecules of biological origin. In particular, atomic force microscopy, used with a variable pulling rate, provides valuable information on the folding/unfolding dynamics of proteins. We propose here two different models able to describe the out-of-equilibrium statistical mechanics of a chain composed of bistable units. These latter represent the protein domains, which can be either folded or unfolded. Both models are based on the Langevin approach and their implementation allows for investigating the effect of the pulling rate and of the device intrinsic elasticity on the chain unfolding response. The theoretical results (both analytical and numerical) have been compared with experimental data concerning the unfolding of the titin and filamin proteins, eventually obtaining a good agreement over a large range of the pulling rates.

中文翻译：

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用于单分子力光谱实验的速率相关力扩展模型。

单分子力光谱技术可以测量生物起源大分子的几种静态和动态特征。特别地，以可变的拉动速率使用的原子力显微镜为蛋白质的折叠/展开动力学提供了有价值的信息。我们在这里提出两个不同的模型，它们能够描述由双稳态单元组成的链的非平衡统计力学。后者代表蛋白质结构域，可以折叠或展开。两种模型均基于Langevin方法，其实现方式可用于研究牵引速率和装置固有弹性对链展开响应的影响。