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Table 2 Effect of single amino acid substitution on MAPK3 group I and II variants stabilitya

From: The complex impact of cancer-related missense mutations on the stability and on the biophysical and biochemical properties of MAPK1 and MAPK3 somatic variants

 

Tm (°C)

\(\Delta G^{{{\text{H}}_{{2}} {\text{O}}}}\) (kcal/mol)

m (kcal/mol/M)

[GdmCl]0.5 (M)

  

CD

([\(\Theta\)]222)

Fluorescence

(\(\overline{{\uplambda }}\))

CD

([\(\Theta\)]222)

Fluorescence

(\(\overline{{\uplambda }}\))

CD

([\(\Theta\)]222)

Fluorescence

(\(\overline{{\uplambda }}\))

NP-WT

46.0

1.84 ± 0.12

2.26 ± 0.14

0.93 ± 0.07

1.11 ± 0.08

1.98

2.04

P-WT

47.1

1.72 ± 0.09

2.40 ± 0.12

0.83 ± 0.04

1.22 ± 0.06

2.07

1.97

NP-E98K

52.0

3.65

2.92

2.92

4.32

4.69 ± 0.88

0.96 ± 0.25

2.86 ± 0.68

1.25 ± 0.56

0.78 ± 0.05

3.03 ± 0.19

1.02 ± 0.04

3.46 ± 0.33

P-E98K

47.1

3.95

3.69

4.66

2.68

3.73 ± 0.29

1.18 ± 0.09

4.48 ± 0.07

0.78 ± 0.01

1.06 ± 0.01

3.12 ± 0.04

1.04 ± 0.02

3.43 ± 0.17

NP-R152W

49.0

2.60

3.84

2.61 ± 0.13

3.55 ± 0.90

0.96 ± 0.60

1.10 ± 0.06

0.73 ± 0.05

3.99 ± 0.71

2.37

P-R152W

42.0

58.0

3.20

3.02

2.12 ± 0.14

4.32 ± 0.84

1.19 ± 0.36

1.00 ± 0.07

0.74 ± 0.06

2.54 ± 0.17

2.11

NP-P336Q

44.0

3.28

3.86

3.52

2.89

4.39 ± 0.88

1.24 ± 0.16

3.75 ± 0.44

0.93 ± 0.08

0.75 ± 0.03

3.11 ± 0.07

0.94 ± 0.02

3.09 ± 0.06

P-P336Q

47.0

2.91

3.08

7.06

3.83

3.03 ± 0.53

1.11 ± 0.16

6.03 ± 0.68

1.57 ± 0.22

0.96 ± 0.03

2.78 ± 0.08

1.17 ± 0.05

2.44 ± 0.05

NP-E339V

46.1

2.83

2.92

5.51

6.43

3.29 ± 0.59

1.06 ± 0.10

5.32 ± 0.75

1.74 ± 0.42

0.86 ± 0.03

2.76 ± 0.05

1.04 ± 0.04

3.70 ± 0.49

P-E339V

48.1

2.80

3.00

7.28

4.19

3.00 ± 0.51

0.94 ± 0.12

6.67 ± 0.12

1.64 ± 0.32

0.94 ± 0.03

3.18 ± 0.08

1.08 ± 0.02

2.55 ± 0.08

  1. aMelting temperatures (Tm) were obtained as described in Materials and Methods by continuously monitoring the molar ellipticity at 222 nm every 0.5 °C. GdmCl-induced unfolding equilibrium data were measured as described in Materials and Methods by monitoring the ellipticity at 222 nm ([Θ222]) and the fluorescence intensity-averaged emission wavelength (λ¯¯¯λ¯, Eq. (2)). ΔGH2O and m values were obtained from Eq. (3); [GdmCl]0.5 was calculated from Eq. (5). [Θ222] and ‾λ data were fitted to Eq. (4) for the 2-state unfolding or to Eq. (6), for the 3-state unfolding. Data are reported as the mean ± SE of the fit. All the measures were performed on the non-phosphorylated (NP-) and phosphorylated (P-) form of the proteins
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Human Genomics

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