Quantifying the Native Energetics Stabilizing Bacteriorhodopsin by Single-Molecule Force Spectroscopy.,Physical Review Letters

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Quantifying the Native Energetics Stabilizing Bacteriorhodopsin by Single-Molecule Force Spectroscopy.
Physical Review Letters ( IF 8.1 ) Pub Date : 2020-08-05 , DOI: 10.1103/physrevlett.125.068102
Hao Yu ₁ , David R Jacobson ₂ , Hao Luo ₁ , Thomas T Perkins _{2,

3}

Affiliation

We quantified the equilibrium (un)folding free energy

Δ G_{0}

of 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 of

Δ G_{0}

via 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,

Δ G_{0}

was determined in bacteriorhodopsin’s native bilayer, an advance over traditional results obtained by chemical denaturation in nonphysiological detergent micelles.

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