TABLE 3.

Parallax quenching data of H-bonded and H-bond free forms of probe F in DOPC vesicles

Probe F form	FTC/F0	F5/F0	F12/F0	Zcf,* Å
H-bonded	0.37	0.42	0.45	16.5
H-bond free	0.63	0.59	0.58	9

F_TC/F₀, F₅/F₀, and F₁₂/F₀ are the values of fluorescence quenching ratios of DOPC vesicles containing 15 mol % TempoPC, 5-SLPC, or 12-SLPC, respectively, to DOPC vesicles lacking nitroxide-labeled lipid. The values were obtained by deconvolution of the fluorescence quenching data obtained previously (Klymchenko et al., 2002). The obtained integral intensities of the H-N^* form and a sum of integral intensities of N^* and T^* forms were used to calculate the quenching for H-bonded and H-bond free forms of probe F.

^*Z_cf is the distance between the middle of the bilayer and the chromophore center calculated from the parallax equation (Abrams and London, 1993).