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摘要翻译：
从非平衡的机械展开操作重建了离晶格模型蛋白质的平衡自由能景观作为内部（反应）坐标的函数。这项任务是通过两种独立的方法完成的：使用扩展版本的Jarzynski等式(EJE)和蛋白质固有结构(ISs)。在“折叠转变”附近的温度范围内，我们发现通过EJE和IS方法获得的自由能之间有很好的定量一致性。这表明这两种方法是一致的，能够再现被测系统的平衡性质。此外，对于所研究的模型，由拉力引起的结构转变可能与折叠的热力学方面有关。
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英文标题：
《Reconstructing the free energy landscape of a mechanically unfolded
model protein》
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作者：
Alberto Imparato, Stefano Luccioli, Alessandro Torcini
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最新提交年份：
2007
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分类信息：
一级分类：Physics 物理学
二级分类：Statistical Mechanics 统计力学
分类描述：Phase transitions, thermodynamics, field theory, non-equilibrium phenomena, renormalization group and scaling, integrable models, turbulence
相变，热力学，场论，非平衡现象，重整化群和标度，可积模型，湍流
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一级分类：Quantitative Biology 数量生物学
二级分类：Biomolecules 生物分子
分类描述：DNA, RNA, proteins, lipids, etc.; molecular structures and folding kinetics; molecular interactions; single-molecule manipulation.
DNA、RNA、蛋白质、脂类等；分子结构与折叠动力学；分子相互作用；单分子操作。
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英文摘要：
The equilibrium free energy landscape of an off-lattice model protein as a function of an internal (reaction) coordinate is reconstructed from out-of-equilibrium mechanical unfolding manipulations. This task is accomplished via two independent methods: by employing an extended version of the Jarzynski equality (EJE) and the protein inherent structures (ISs). In a range of temperatures around the ``folding transition'' we find a good quantitative agreement between the free energies obtained via EJE and IS approaches. This indicates that the two methodologies are consistent and able to reproduce equilibrium properties of the examined system. Moreover, for the studied model the structural transitions induced by pulling can be related to thermodynamical aspects of folding.
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PDF链接：
https://arxiv.org/pdf/705.3256
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