Table 2.
Results for the four most designable distinct folds for the model four-helix bundles shown in Fig. 4
| Structure | Sequence | Energy gap, kBT | Minimum mutations |
|---|---|---|---|
| a helix 1 | PPHHHHHHPHHPPHH | 6.65 | 4 |
| a helix 2 | HHPPHHPHHPHPHHP | ||
| a helix 3 | PPHHPPHHPHHHHHH | ||
| a helix 4 | PHHPPHHPHHPHPHP | ||
| b helix 1 | HHPPHHPHHPHHHHP | 5.85 | 3 |
| b helix 2 | HHHPPHHPHHHPHHP | ||
| b helix 3 | PPHHHHHPHPPPHHP | ||
| b helix 4 | HPHHHPHHPHHPHHH | ||
| c helix 1 | HHHHPPHPPPHPPHP | 8.3 | 5 |
| c helix 2 | PHPPHHPPPHPPHHP | ||
| c helix 3 | PHPPHHHPPHHPPPP | ||
| c helix 4 | PPPPHPPPHPPHHHH | ||
| d helix 1 | HPHHHPHHPPHHHPP | 4.70 | 3 |
| d helix 2 | PHHPHHHPHHPPPHP | ||
| d helix 3 | PHHPHHHPHHPHHPP | ||
| d helix 4 | PHHHPHHPHHHHHHH |
Column 2 gives the optimized hydrophobic-polar patterning of each of the length 15 helices. For these sequences, the third column gives the energy gap in kBT to the nearest distinct structural competitor. The last column gives the minimum number of point mutations necessary to reduce the energy gap to zero.