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. Author manuscript; available in PMC: 2013 Jul 1.
Published in final edited form as: Biochim Biophys Acta. 2012 Jul;1818(7):10.1016/j.bbamem.2012.03.011. doi: 10.1016/j.bbamem.2012.03.011

Table 2.

Values of the apparent dissociation constant Kd and calculated apparent free energy of binding, ΔG. The tabulated values were obtained from fluorescence anisotropy data and Equations 1 and 2. Standard error for each value of ΔG was 0.1 kcal/mol.

Peptides Kd (μM) (for 30% PG SUV) ΔG (kcal/mol)
S4-W 174 ± 28 −5.1
W-S4 132 ± 21 −5.3
S4(F9W, W18F) 73 ± 13 −5.6
S4-W(R10−1) 279 ± 32 −4.9
S4-W(R10−2) 496 ± 51 −4.5
S4-W(R7,10−2) 286 ± 41 −4.8
S4-W(R4,7,10−2) 241 ± 35 −4.9
S4-W(R4,7,10,13−2) 234 ± 39 −4.9
S4-W(Rregain−2) 172 ± 22 −5.1
S4-W (F9P) 696 ± 122 −4.3