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Table 5 Average a-helix contents (%) from DSSP analysis for 1mof, 1mof-I54D, 2wrp, and 2wrp-H16I at different temperatures

From: A hydrophobic spine stabilizes a surface-exposed α-helix according to analysis of the solvent-accessible surface area

whole protein

 

300 K

p-value

400 K

p-value

500 K

p-value

1mof

51.27

>0.001

22.46

>0.001

4.80

>0.001

1mof-I54D

43.38

21.81

5.42

2wrp

65.44

>0.001

48.03

>0.001

4.62

>0.001

2wrp-H16I

61.51

42.41

13.86

hydrophobic spine regions

1mof

30.85

>0.001

11.61

>0.001

3.64

>0.001

1mof-I54D

29.95

10.20

1.61

 

2wrp

13.71

>0.001

11.52

>0.001

1.30

0.84

2wrp-H16I

13.26

12.29

1.12

  1. The boldface indicates the significant difference after Bonferroni correction