TY - JOUR
AU - Hao Yu
AU - David Jacobson
AU - Hao Luo
AU - Thomas Perkins
AB - We quantified the equilibrium (un)folding free energy ΔG0 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 ΔG0 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, ΔG0 was determined in bacteriorhodopsin’s native bilayer, an advance over traditional results obtained by chemical denaturation in nonphysiological detergent micelles.

BT - Physical Review Letters
DA - 2020-08
DO - 10.1103/PhysRevLett.125.068102
N2 - We quantified the equilibrium (un)folding free energy ΔG0 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 ΔG0 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, ΔG0 was determined in bacteriorhodopsin’s native bilayer, an advance over traditional results obtained by chemical denaturation in nonphysiological detergent micelles.

PB - American Physical Society
PY - 2020
SE - 068102
EP - 068102
T2 - Physical Review Letters
TI - Quantifying the native energetics stabilizing bacteriorhodopsin by single-molecule force spectroscopy
UR - https://link.aps.org/doi/10.1103/PhysRevLett.125.068102
VL - 125
ER -