. Author manuscript; available in PMC: 2016 Nov 1.

Published in final edited form as: Biochim Biophys Acta. 2015 Sep 2;1848(11 0 0):2767–2778. doi: 10.1016/j.bbamem.2015.09.003

Table 2.

Summary of PMF analysis

Simulation	Position of energy minimum relative to bilayer center (nm)	Depth of PMF well ± S.E. (kJ/mol)^†	ΔG^bind ± S.E. (kJ/mol)^*
CG-pmf-WT	2.35	−57.8 ± 0.7	−23.2 ± 0.3
CG-pmf-K8E	2.5	−55.2 ± 1.3	−21.7 ± 0.7
CG-pmf-K15E	2.35	−65.8 ± 0.5	−26.8 ± 0.3
CG-pmf-K20E	2.5	−57.9 ± 0.8	−23.3 ± 0.4
CG-pmf-K22E	2.35	−59.3 ± 1.3	−24.0 ± 0.7
CG-pmf-K25E	2.5	−49.5 ± 0.7	−18.1 ± 0.4
CG-pmf-K28E	2.35	−49.3 ± 0.4	−18.8 ± 0.2
AT-pmf-WT	1.7	−61.2 ± 4.5	n.t.
AT-pmf-K15E	1.7	−72.2 ± 4.7	n.t.
AT-pmf-K28E	2.1	−40.1 ± 5.0	n.t.

n.t. = not tested

^†

For the AT series, the PMF depth relative to the PMF value at z = 3.8 nm is shown. The mean force at this position was smaller than 3.0 kJ/nm and our estimation based on the CG PMF curve suggested that the systematic error in the PMF depth resulting from ignoring the z = 3.8 – 5.0 nm range was smaller than 0.5 kJ/mol for all three peptides.