Table 1 Properties of the Amino acids used in the present study.

From: Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements

Amino acid

M X (Da)

B X

\({{\boldsymbol{\Delta }}}_{{\boldsymbol{X}}}^{{\boldsymbol{\min }}}\)

\({{\boldsymbol{P}}}_{{\boldsymbol{X}}}^{{\bf{\max }}}\) (%)

N X

W X

I X

Ala

71.079

4

1.176°

0.437

113609

496.654

0.143

Arg

156.188

10

1.593°

0.265

45373

120.333

1.298

Asn

114.104

2

2.535°

0.156

46573

72.701

1.569

Asp

115.089

1

2.169°

0.192

56963

109.191

1.054

Cys

103.139

5

2.951°

0.173

15823

27.298

3.778

Gln

128.131

2

2.118°

0.307

35633

109.470

1.170

Glu

129.116

1

1.748°

0.321

48458

155.431

0.831

Gly

57.052

5

2.118°

0.124

98983

122.840

0.464

His

137.141

13

2.609°

0.173

27675

47.910

2.862

Ile

113.159

7

1.488°

0.285

74768

213.090

0.531

Leu

113.159

7

1.463°

0.276

116941

322.560

0.351

Lys

128.174

10

1.856°

0.276

40135

110.584

1.159

Met

131.193

7

1.782°

0.284

20968

59.610

2.201

Phe

147.177

11

2.169°

0.190

56511

107.242

1.372

Pro

97.117

4

2.222°

0.110

54555

60.167

1.614

Ser

87.078

4

1.978°

0.141

66612

93.593

0.930

Thr

101.105

6

2.069°

0.178

68557

121.726

0.831

Trp

186.213

14

2.687°

0.200

21118

42.340

4.398

Tyr

163.176

11

2.400°

0.184

48972

90.250

1.808

Val

99.133

4

1.622°

0.241

95564

230.082

0.431

  1. M X is the residue average mass (without water). B X gives Davis’ biosynthetic steps37. \({{\rm{\Delta }}}_{X}^{min}(deg)\) is the optimal bin angle determined by MISE method17. \({P}_{X}^{{\rm{\max }}}\) corresponds to the peak of the Ramachandran distribution P X (ϕ, ψ). N X is the number of points used for determining P X (ϕ, ψ). \({W}_{X}={P}_{X}^{{\rm{\max }}}\times {N}_{X}\) is an estimator of the maximum possible observations at the most frequent conformation. I X  = M X /W X is the mutational inertia.
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