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. 2001 Aug 15;29(16):3311–3319. doi: 10.1093/nar/29.16.3311

Table 1. Equilibrium dissociation constants of CREB–CRE and CREB–AP-1 complexes at 25°C determined by electrophoretic mobility shift analysis.

Peptide
ΔGCRE24 (kcal·mol–1)
ΔGAP-123 (kcal·mol–1)
ΔΔGCREGmut – ΔGB70) (kcal·mol–1)
ΔΔGAP-1Gmut – ΔGB70) (kcal·mol–1)
ΔΔGspec (kcal·mol–1)
B70 –21.5 ± 0.1 –19.0 ± 0.2     –2.5 ± 0.2
Q6A –24.0 ± 0.2 –21.9 ± 0.1 –2.5 –2.9 –2.1 ± 0.3
E9A –25.0 ± 0.2 –21.9 ± 0.3 –3.5 –2.9 –3.1 ± 0.1
E10A –22.4 ± 0.2 –20.5 ± 0.3 –0.9 –1.5 –1.9 ± 0.1
R13A –23.8 ± 0.5 –20.7 ± 0.1 –2.3 –1.7 –3.1 ± 0.5
K14A –24.6 ± 0.4 –21.1 ± 0.3 –3.1 –2.1 –3.5 ± 0.6
R15A –24.7 ± 0.4 –21.5 ± 0.1 –3.2 –2.5 –3.2 ± 0.3
E16A –23.4 ± 0.1 –20.8 ± 0.1 –1.9 –1.8 –2.6 ± 0.1
V17A –23.6 ± 0.1 –19.8 ± 0.2 –2.1 –0.8 –3.8 ± 0.3
R18A –24.3 ± 0.3 –20.8 ± 0.3 –2.8 –1.8 –3.5 ± 0.1
L19A –25.2 ±0.1 –22.4 ± 0.4 –3.7 –3.4 –2.8 ± 0.2
M20A –23.7 ± 0.2 –21.6 ± 0.2 –2.2 –2.6 –2.1 ± 0.2
K21A –25.1 ± 0.6 –20.1 ± 0.2 –3.6 –1.1 –5.0 ± 0.5
R23A –26.3 ± 0.4 –21.5 ± 0.1 –4.8 –2.5 –4.8 ± 0.3
E24A –24.2 ± 0.1 –22.9 ± 0.1 –2.7 –3.9 –1.3 ± 0.1
R27A –23.6 ± 0.3 –20.4 ± 0.1 –2.1 –1.4 –3.2 ± 0.3
E28A –23.5 ± 0.2 –22.0 ± 0.2 –2.0 –3.0 –1.5 ± 0.1
R31A –21.4 ± 0.1 –18.3 ± 0.2 +0.1 +0.7 –3.1 ± 0.2
K32A –20.8 ± 0.3 –18.0 ± 0.2 +0.7 +1.0 –2.8 ± 0.5
K33A –21.6 ± 0.1 –18.1 ± 0.1 –0.1 +0.9 –3.5 ± 0.1
K34A –23.4 ± 0.2 –19.9 ± 0.6 –1.9 –0.9 –3.5 ± 0.4
E35A –20.5 ± 0.1 –19.0 ± 0.1 +1.0 0 –1.5 ± 0.05
V37A –22.0 ± 0.3 –19.3 ± 0.3 –0.5 –0.3 –2.7 ± 0.3
C39A –25.1 ± 0.1 –23.0 ± 0.03 –3.6 –4.0 –2.1 ± 0.1
E41A –22.5 ± 0.1 –21.2 ± 0.2 –1.0 –2.2 –1.3 ± 0.1
N42A –23.3 ± 0.2 –20.8 ± 0.3 –1.8 –1.8 –2.5 ± 0.1
E48A –24.2 ± 0.3 –22.5 ± 0.3 –2.7 –3.5 –1.7± 0.3

All values represent the average ± SE of at least three independent determinations. Values of ΔG were calculated from the equation ΔG = –RTlnKapp–1, where Kapp is the equilibrium dissociation constant, R = 1.987 × 103 kcal·mol–1·K–1 and T is the temperature in Kelvin.