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Table 3 Spectrum of mutations appearing in α-helix, β-strand, turn and bend structures, expected values are calculated from mutated and mutant amino acid composition in the studied proteinsa

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 148 136 1.07 3.00E-01 58 67 1.15 2.84E-01
C 54 64 1.43 2.32E-01 117 107 0.94 3.32E-01
D 81 79 0.06 8.06E-01 112 125 1.28 2.57E-01
E 96 91 0.29 5.91E-01 71 68 0.18 6.75E-01
F 53 53 0.00 9.91E-01 77 72 0.29 5.87E-01
G 220 198 2.48 1.15E-01 95 85 1.12 2.91E-01
H 63 70 0.69 4.05E-01 91 87 0.20 6.57E-01
I 83 80 0.14 7.05E-01 55 64 1.36 2.44E-01
K 43 45 0.09 7.61E-01 92 88 0.21 6.43E-01
L 188 186 0.03 8.70E-01 96 91 0.29 5.91E-01
M 65 63 0.08 7.74E-01 48 78 11.54*** 6.79E-04
N 60 72 2.12 1.46E-01 61 60 0.04 8.47E-01
P 68 76 0.76 3.82E-01 170 156 1.25 2.63E-01
Q 45 50 0.47 4.91E-01 89 92 0.13 7.17E-01
R 299 280 1.31 2.53E-01 196 179 1.71 1.91E-01
S 78 101 5.05* 2.46E-02 144 140 0.12 7.31E-01
T 62 68 0.46 4.99E-01 119 109 0.85 3.57E-01
V 122 118 0.12 7.28E-01 138 149 0.78 3.77E-01
W 44 44 0.00 9.72E-01 56 62 0.57 4.51E-01
Y 67 68 0.00 9.46E-01 54 61 0.83 3.62E-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.