Table 1 Physicochemical attributes used in the study
From: A strategy to select suitable physicochemical attributes of amino acids for protein fold recognition
No. | Attributes | Symbols |
|---|---|---|
1 | Hydrophibicity (membrane buried helix) [36] | H |
2 | Polarity [37] | P |
3 | Polarizability parameter [38] | Z |
4 | Normalized frequency of alpha-helix [39] | X |
5 | Normalized van der Waals volume [40] | V |
6 | alpha-NH chemical shifts [41] | S |
7 | A parameter of charge transfer capability [42] | C |
8 | The Kerr-constant increments [43] | K |
9 | Normalized hydrophobicity scales for beta-proteins [44] | B |
10 | Normalized frequency of beta-sheet [45] | F |
11 | Normalized frequency of beta-turn [45] | T |
12 | Normalized frequency of reverse turn, with weights [46] | R |
13 | Size [47] | E |
14 | Amino acid composition [48] | A |
15 | Frequency of the 1st residue in turn [45] | F |
16 | Spin-spin coupling constants 3JHalpha-NH [41] | N |
17 | Relative mutability [49] | M |
18 | Direction of hydrophobic moment [50] | D |
19 | Molecular weight [51] | W |
20 | Optical rotation [51] | O |
21 | Aperiodic indices for alpha-proteins [52] | a |
22 | Aperiodic indices for beta-proteins [52] | b |
23 | Aperiodic indices for alpha/beta-proteins [52] | c |
24 | Volume [53] | U |
25 | Partition energy [54] | I |
26 | Heat capacity [55] | Q |
27 | Absolute entropy [55] | L |
28 | Average accessible surface area [56] | G |
29 | Percentage of buried residues [56] | J |
30 | Percentage of exposed residues [56] | Y |