Table 3 The protein folding stability changes of 11 missense mutations.

From: Analysis of SARS-CoV-2 mutations in the United States suggests presence of four substrains and novel variants

Rank

Mutation

Protein

ΔΔG(kcal/mol)

\({R}_{8}^{w}\)

\({R}_{8}^{m}\)

\(\Delta {\bar{R}}_{8}\)%

\(\langle {C}_{s}^{w}\rangle\)

\(\langle {C}_{s}^{m}\rangle\)

\(\Delta \langle {\bar{C}}_{s}\rangle\)%

Top 1

23403A>G-(D614G)

S protein

0.34

10.27

10.10

1.7

2376

1386

42

Top 2

14408C>T-(P323L)

NSP12(RdRp)

−0.11

9.77

9.87

−1.0

1105

1959

−77

Top 3

25563G>T-(Q57H)

ORF3a

−0.24

11.33

11.66

−1.5

25,061

58,592

−134

Top 4

1059C>T-(T85I)

NSP2

−0.05

12.37

12.51

−1.1

89,764

166,399

−85

Top 5

28881G>A-(R203K)

Nucleocapsid

−1.14

15.69

15.44

1.6

19,356,251

9,436,565

51

Top 6

28883G>C-(G204R)

Nucleocapsid

−1.56

14.99

16.94

13

1,193,960

1,191,199,736

−99,669

Top 7

28882G>A-(R203K)

Nucleocapsid

−1.14

15.69

15.44

1.6

19,356,251

9,436,565

51

Top 8

28144T>C-(L84S)

ORF8

−0.99

12.28

12.05

1.9

12,810

6504

49

Top 9

17858A>G-(Y541C)

NSP13(Helicase)

−0.81

11.52

10.40

9.7

506,640

7271

99

Top 10

17747C>T-(P504L)

NSP13(Helicase)

−0.59

7.52

7.54

0.3

4668

6094

−31

Top 11

27964C>T-(S24L)

ORF8

0.20

11.72

11.66

0.5

11,685

29,777

−155

  1. The folding stability change ΔΔG = ΔGw − ΔGm, where ΔGw and ΔGm are the folding free energies of the wild type and the mutant type, respectively. \({R}_{8}^{{\mathrm{w}}}\) and \({R}_{8}^{{\mathrm{m}}}\) are FRI rigidities for the wild type and mutant type of the protein with η = 8 Å. Here, \(\langle {C}_{s}^{{\mathrm{w}}}\rangle\) and \(\langle {C}_{s}^{{\mathrm{m}}}\rangle\) are the average subgraph centralities of the wild type and the mutant type, respectively. \(\Delta {\bar{R}}_{8}\) and \(\Delta \langle {\bar{C}}_{s}\rangle\) are the molecular FRI rigidity changes and the average subgraph centrality change.