TABLE 3.

Binding parameters of αS variant interactions with gel state DPPC SUVs

S.E. values are reported for experiments using independent SUV preparations in 10 mm KH₂PO₄/K₂HPO₄ (pH 7.4) and 100 mm KCl. Thermodynamic parameters were obtained at 30 °C.

αS variant	ΔH	TΔS	ΔG	KDa	na
	kcal/mol	kcal/mol	kcal/mol	×10−6m
αS	−399.9 ± 25.7	−389.7 ± 25.7	−10.2 ± 0.1	0.039 ± 0.001	292 ± 14
αS(Cys11–Cys83)	−24.6 ± 5.9	−17.4 ± 5.6	−7.2 ± 0.2	6.03 ± 2.1	76 ± 16
αS(Cys11–Cys81)	−340.0 ± 3.6	−330.0 ± 3.6	−10.0 ± 0.1	0.055 ± 0.001	240 ± 3

^a K_D denotes the apparent dissociation constant, and n is the number of protein-associated lipids (Equations 3 and 4).