Table 6 Selected R values between some interesting physicochemical properties and the optimized SSM of amino acids.

R: 0.76

KUMS000103 Distribution of amino acid residues in the α-helices in thermophilic proteins

0.54

PRAM900102 Relative frequency in α-helix

-0.42

MUNV940102 Free energy in α-helical region

Hydrophilicity

Hydrophilic

2

R (0.38

0.27

0.16

0.02)

R: 0.38

HOPT810101 Hydrophilicity value

0.16

KUHL950101 Hydrophilicity scale

Hydrophobicity

Hydrophobic

36

R (0.35

-0.09

-0.30

0.03)

R: 0.35

LEVM760101 Hydrophobic parameter

-0.13

CIDH920103 Normalized hydrophobicity scales for α+β-proteins

-0.30

CASG920101 Hydrophobicity scale from native protein structures

Turn

Turn

26

R (0.38

-0.22

-0.57

0.06)

R: 0.38

OOBM850102 Optimized propensity to form reverse turn

-0.19

PALJ810116 Normalized frequency of turn in α/β class

-0.57

ROBB760108 Information measure for turn

Charge

Charge

5

R (0.59

-0.01

-0.43

0.2)

R: 0.59

FAUJ880112 Negative charge

-0.07

FAUJ880111 Positive charge

-0.43

CHAM830108 A parameter of charge transfer donor capability

Thermophile

thermophile

6

R (0.76

0.52

0.33

0.2)

R: 0.76

KUMS000103 Distribution of amino acid residues in the α-helices in thermophilic proteins

0.56

FUKS010109 Entire chain composition of amino acids in intracellular proteins of thermophiles (percent)

0.33

FUKS010105 Interior composition of amino acids in intracellular proteins of thermophiles (percent)