Table 1 Φbinding values for the interaction between wild type and mutants of ACTRWT and NCBDY2108W, respectively, measured in 20 mM phosphate (pH = 7.4), 150 mM NaCl and 277 K
From: The transition state structure for coupled binding and folding of disordered protein domains
ACTRWT | NCBDY2108W | ||||
|---|---|---|---|---|---|
NCBDY2108W mutant | ΔΔGEq kcal/mol | Φbinding | ACTR mutant | ΔΔGEq kcal/mol | Φbinding |
I2062V α1 | 0.20 ± 0.01 | −0.12 ± 0.07 | L1048A α1 | 1.02 ± 0.02 | 0.27 ± 0.02 |
V2086A α2 | 0.73 ± 0.02 | −0.04 ± 0.02 | L1049A α1 | 1.30 ± 0.02 | 0.17 ± 0.02 |
L2087A α2 | 2.2 ± 0.1 | 0.14 ± 0.03 | L1055A α1 | 0.46 ± 0.05 | 0.85 ± 0.10 |
L2096A α3 | 1.9 ± 0.1 | 0.16 ± 0.03 | L1056A α1 | 2.09 ± 0.1 | 0.07 ± 0.02 |
I2101Va α3 | 0.01 ± 0.02 | – | A1061Ga loop | 0.08 ± 0.06 | – |
V2109A α3 | −0.17 ± 0.02 | 0.22 ± 0.09 | I1067V α2 | 0.62 ± 0.02 | 0.16 ± 0.02 |
I1073V α3 | 0.68 ± 0.03 | 0.15 ± 0.05 | |||
V1077A α3 | −0.19 ± 0.02 | −0.01 ± 0.13 | |||
