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Table 4 Spectrum of mutations appearing in α-helix, β-strand, turn and bend structures. Expected values are calculated from amino acid composition in secondary structural elementsa

From: Spectrum of disease-causing mutations in protein secondary structures

Amino acid Original residues Expected residues χ2 P value Mutant residues Expected residues χ2 P value
A 148 139 0,53 4.66E-01 58 119 31.05*** 2.51E-08
C 54 32 15,50*** 6.82E-05 117 69 32.93*** 9.58E-09
D 81 96 2,34 1.26E-01 112 79 13.64*** 2.21E-04
E 96 147 17,60*** 2.71E-05 71 69 0.04 8.33E-01
F 53 87 13,51*** 2.36E-04 77 79 0.06 8.10E-01
G 220 136 52,47*** 4.48E-13 95 114 3.10 7.85E-02
H 63 48 5,06* 2.47E-02 91 79 1.78 1.83E-01
I 83 110 6,51** 1.07E-02 55 104 23.00*** 1.62E-06
K 43 113 43,42*** 4.37E-11 92 69 7.47** 6.26E-03
L 188 205 1,34 2.46E-01 96 163 27.69*** 1.42E-07
M 65 49 5,02* 2.51E-02 48 45 0.27 6.02E-01
N 60 69 1,10 2.93E-01 61 79 4.16* 4.14E-02
P 68 67 0,02 8.98E-01 170 119 22.16*** 2.51E-06
Q 45 82 16,87*** 3.98E-05 89 69 5.63* 1.76E-02
R 299 119 272,51*** 3.43E-61 196 168 4.60* 3.19E-02
S 78 104 6,60** 1.01E-02 144 183 8.32** 3.92E-03
T 62 92 10,03** 1.53E-03 119 119 0.00 9.79E-01
V 122 144 3,33 7.01E-02 138 119 3.13 7.67E-02
W 44 30 6,27** 1.23E-02 56 35 13.20*** 2.81E-04
Y 67 70 0,15 6.95E-01 54 59 0.48 4.87E-01
Sum 1939 1939    1939 1939   
  1. aχ2-numbers in italics indicate underrepresentation and numbers in bold overrepresentation compared to random distribution based on amino acid frequencies. The results of the χ2 are shown with significance level: * P < 0.05; ** P < 0.01; *** P < 0.001.