Quantifying the Native Energetics Stabilizing Bacteriorhodopsin by Single-Molecule Force Spectroscopy
Quantifying the Native Energetics Stabilizing Bacteriorhodopsin by Single-Molecule Force Spectroscopy
复制标题
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
复制
发表时间:
2020
影响因子:
8.6
通讯作者:
Perkins Thomas T.
中科院分区:
文献类型:
--
作者:
Yu Hao;Jacobson David R.;Luo Hao;Perkins Thomas T.
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.