用单分子实验重构多蛋白质的自由能谱
Reconstructing the free energy landscape of a polyprotein by single-molecule experiments
摘要：
利用原子力显微镜研究了由Ig27的8个结构域组成的工程蛋白的机械去折叠。利用涨落关系，作为分子伸长的函数的平衡自由能估计从拉伸实验。这样的自由能表现出规则的形状，其在零力下设定20 nm量级的典型展开长度。这个长度尺度原来是远大于动力学展开长度，也是通过分析动态载荷下的分子的典型断裂力估计。
英文摘要：
The mechanical unfolding of an engineered protein composed of eight domains of Ig27 is investigated by using atomic force microscopy. Exploiting a fluctuation relation, the equilibrium free energy as a function of the molecule elongation is estimated from pulling experiments. Such a free energy exhibits a regular shape that sets a typical unfolding length at zero force of the order of 20 nm. This length scale turns out to be much larger than the kinetic unfolding length that is also estimated by analyzing the typical rupture force of the molecule under dynamic loading.
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