Table 1.
The fractional helicity fH (%) and the corresponding number of helical residues (n) of each Skn protein and the corresponding complexes
| Protein | Free protein
|
Complex
|
Tm, °C | ||
|---|---|---|---|---|---|
| fH, % | n | fH, % | n | ||
| N5-C85 | 30.0 | 25.0 | 60.0 | 49.0 | 70.9 |
| N5-C80 | 32.0 | 25.0 | 63.0 | 49.0 | 72.9 |
| N5-C77 | 31.0 | 23.0 | 56.0 | 43.0 | 70.9 |
| N5-C74 | 32.0 | 23.0 | 51.0 | 36.0 | 67.0 |
| N5-C71 | 37.0 | 25.0 | — | — | — |
| N5-C64 | 41.0 | 27.0 | — | — | — |
Three helical segments were assumed for the free proteins, and four were assumed for the bound proteins. Although changing the number of helices would change the calculated numbers slightly, conclusions drawn from the comparisons between the different proteins should be reliable as long as the proteins in question contain the same number of helical segments. The melting temperatures (Tm) of the specific complexes are shown in the last column (26).