TABLE 2.

	TM orientation	Surface orientation
ΔGtot* (kT)	−10.2 ± 5.6	−7.4 ± 13.4
ΔGcon† (kT)	−5.4 ± 5.6	−3.3 ± 11.6
ΔE‡ (kT)	−35 ± 5	−14.4 ± 9.6
−TΔScon§ (k)	29.6 ± 2.6	11.1 ± 6.6
ΔGSIL¶ (kT)	−7.6 ± 0.1	−4.3 ± 2.5
ΔGSIL_b‖ (kT)	8.35 ± 0.12	3.5 ± 1.2
ΔGSIL_s** (kT)	−15.91 ± 0.01	−7.8 ± 3.7
ΔGdef†† (kT)	2.8 ± 0.06	0.2 ± 0.2
〈z〉‡‡ (Å)	11.53 ± 0.04	15.4 ± 0.4
abs(zc)§§ (Å)	1.6 ± 0.2	24.6 ± 3.2
〈θ〉¶¶ (°)	13.95 ± 0.3	86 ± 3.2

Thermodynamic parameters for the membrane association of M2δ in TM and surface orientations. The values represent the average obtained after equilibration.

^*Total free energy (ΔG_tot).

^†ΔG_con = ΔE − TΔS_con.

^‡Internal energy, calculated with reference to 〈E_aq〉 = 49 kT.

^§The conformational entropy component.

^¶Total external free energy, including peptide solvation and immobilization and lipid perturbation effects: ΔG_SIL = ΔG_sol + ΔG_imm + ΔG_lip.

^‖Backbone external free energy.

^**Sidechain external free energy.

^††Membrane deformation free energy.

^‡‡The width of a monolayer.

^§§Absolute value of the z-coordinate of the centroid of the chain; midplane of the membrane is at z = 0.

^¶¶The projection angle of the peptide's end-to-end distance vector r and the membrane normal z. The values in parentheses depict the standard deviation of different runs for given case.