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. Author manuscript; available in PMC: 2020 Jul 23.
Published in final edited form as: J Struct Biol. 2010 Feb 20;170(2):216–225. doi: 10.1016/j.jsb.2010.02.013

TABLE 1.

Thermal stability parameters of B-ZIP domains with arylstibonic acids

NSC13746
Protein Compound conc., μM Tma,°C ΔHm, kcal mol−1 ΔGDib, kcal mol−1
Kaapp(Tm)c
c-Fos|JunD 0 42.5 −45 ± 5 −8.5 ± 0.1
(AP1) 100 66.1 −58 ± 6 −12.6 ± 0.4 6.0 ×106
VBP 0 50.7 −51 ± 6 −9.8 ± 0.2
100 63.5 −59 ± 7 −12.4 ± 0.3 3.3 ×105
C/EBPα 0 45.8 −56 ± 2 −9.2 ± 0.1
100 62.7 −65 ± 7 −12.6 ± 0.5 1.7 ×106
C/EBPβ 0 64.4 −71 ± 4 −13.4 ± 0.1
100 82.4 −77 ± 6 −17.5 ± 0.5 4.9 ×106
CREB 0 49.3 −53 ± 5 −9.7 ± 0.1
100 77.6 −59 ± 5 −14.5 ± 0.3 6.2 ×108
NSC13782
c-Fos|JunD 0 42.5 −45 ± 5 −8.5 ± 0.1
(AP1) 100 44.7 −47 ± 4 −8.7 ± 0.1 5.9 ×103
VBP 0 50.7 −51 ± 6 −9.8 ± 0.2
100 56.2 −54 ± 5 −10.8 ± 0.2 2.6 ×104
C/EBPβ 0 64.4 −71 ± 4 −13.4± 0.1
100 65.2 −69 ± 5 −13.5 ± 0.5 -
a

The values represent mean of three independent experiments. Error in Tm values was ≤1°C.

b

The error in the ΔGDi value is due to error in ΔHm and ΔCp (1.2 ± 0.2 kcal mol−1) values.

c

Binding constants of compounds for each protein were calculated using equation 3.

Superscript ‘app’ represents the apparent values.