Table 3.
Secondary Structure |
% HOA residues | Number of HOA residues |
Alpha-helix | 7.73 | 672 |
Strand | 3.11 | 271 |
Beta Bridge | 0.21 | 18 |
3–10 helix | 3.86 | 336 |
Bend | 21.50 | 1874 |
Turn | 30.40 | 2650 |
Coil | 33.00 | 2870 |
For each tripeptide environment, (central) residue with highest ASA is selected and distribution of such residues in various secondary structures is calculated.