Quantifying the Native Energetics Stabilizing Bacteriorhodopsin by Single-Molecule Force Spectroscopy

Quantifying the Native Energetics Stabilizing Bacteriorhodopsin by Single-Molecule Force Spectroscopy
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通过单分子力谱定量稳定细菌视紫红质的天然能量

DOI:
10.1103/physrevlett.125.068102
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发表时间:
2020
影响因子:
8.6
通讯作者:
Perkins Thomas T.
Perkins Thomas T.
中科院分区:
物理与天体物理1区
文献类型:
--
作者:
Yu Hao;Jacobson David R.;Luo Hao;Perkins Thomas T.

文献摘要

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我们用单分子力谱法从细菌视紫红质模型的完全折叠状态出发,定量了8个氨基酸区域的平衡(非)折叠自由能。平衡和非平衡数据的分析产生了一致的,高精度的测定通过多种技术(力依赖动力学,克鲁克斯波动定理,逆玻尔兹曼分析)。我们还推导出了该地区自由能景观的完整一维投影。重要的是,确定在细菌视紫红质的天然双层,在非生理洗涤剂胶束中通过化学变性获得的传统结果的进步。
We quantified the equilibrium (un)folding free energyof an eight-amino-acid region starting from the fully folded state of the model membrane-protein bacteriorhodopsin using single-molecule force spectroscopy. Analysis of equilibrium and nonequilibrium data yielded consistent, high-precision determinations ofvia multiple techniques (force-dependent kinetics, Crooks fluctuation theorem, and inverse Boltzmann analysis). We also deduced the full 1D projection of the free-energy landscape in this region. Importantly,was determined in bacteriorhodopsin’s native bilayer, an advance over traditional results obtained by chemical denaturation in nonphysiological detergent micelles.