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. 2020 Aug 4;38(1):152–167. doi: 10.1093/molbev/msaa198

Table 3.

Global Stability of PDZ3 Domains.

PDZ3 [Urea]50%a (M) ΔGD-Na (kcal mol−1) [Urea]50%b (M) ΔGD-Nb (kcal mol−1) m D-N b (kcal mol−1 M−1)
H. sapiens 6.2±0.4 7.6±1.3 6.5±0.4 6.3±1.3 1.0±0.2
S. kowalevskii 2.7±0.1 3.3±0.9 2.7±0.1 4.3±0.9 1.6±0.3
D. melanogaster 2.1±0.1 2.6±0.3 2.1±0.1 2.4±0.3 1.2±0.1
D. melanogaster α3 3.0±0.1 4.0±0.4c 3.0±0.04 4.4±0.3 1.5±0.1
D. ponderosae 3.7±0.1 4.5±0.8 3.7±0.1 5.1±0.8 1.4±0.2
D. ponderosae α3 4.5±0.1 6.0±0.6c 4.4±0.05 7.2±0.7 1.6±0.2
L. loa 4.1±0.1 5.0±1.4 4.0±0.1 7.0±1.4 1.7±0.3
L. loa α3 5.7±0.1 7.7±0.7c 5.8±0.2 6.6±1.4 1.1±0.2
O. bimaculoides 3.1±0.1 3.8±0.8 3.2±0.1 4.6±0.8 1.5±0.3
H. vulgaris 2.9±0.1 3.6±0.8 2.9±0.1 3.9±0.8 1.3±0.3
Bilateria 5.2±0.2 6.4±0.6 5.4±0.2 4.1±0.6 0.8±0.1
Bilateria AltAll 5.75±0.03 7.1±0.3 5.78±0.04 6.8±0.3 1.17±0.05
Protostomia 5.1±0.1 6.3±1.2 5.1±0.1 6.4±1.2 1.2±0.2
Protostomia AltAll 5.3±0.2 6.5±1.4 5.3±0.2 5.9±1.4 1.1±0.3
Deuterostomia 6.0±0.1 7.4±0.6 6.1±0.1 7.1±0.6 1.2±0.1
Deuterostomia AltAll 4.7±0.1 5.8±0.9 4.7±0.1 5.1±0.9 1.1±0.2
Hexapoda 7.0±0.7 10±4.0d 6.7±0.4 17±13 2.5±2.0
Hexapoda AltAll 5.2±0.3 7.4±2.8d 5.3±0.4 5.8±3.0 1.1±0.5
1R 6.1±0.2 7.5±2.4 5.9±0.2 9.4±2.3 1.6±0.4
1R AltAll e 6.6±0.5 13±7.2 1.9±1.1

Note.—Global stability of PDZ3 domains was determined by urea denaturation experiments monitored by circular dichroism at 222 nm (see fig. 6). Experimental data were fitted to a two-state model for denaturation to obtain the concentration of urea, where 50% of the protein is denatured ([Urea]50%), the cooperativity of the unfolding (mD-N value) and the stability (ΔGD-N) as the product of [Urea]50%.and mD-N.

a

The mD-N value was shared among the data sets in the curve fitting; mD-N=1.23 kcal mol−1 M−1.

b

Free fitting of both [Urea]50% and mD-N.

Exceptions: cα3 PDZ3 mD-N=1.35 kcal mol−1 M−1; dHexapoda and Hexapoda AltAll mD-N=1.43 kcal mol−1 M−1; and e1R AltAll.