TABLE 1.
Secondary structural analysis of the Scy I peptide in various membrane-mimicking environments using CDSSTR with a 42-reference protein set*
| Secondary structure (%)*
| |||||||
|---|---|---|---|---|---|---|---|
| Environment | Helix | Strand | Turn | Unrd | RMSD | R1† | R2† |
| Phosphate buffer, pH 7.2 | 0 | 32.8 | 15.9 | 52.7 | 0.134 | 4.67 | −0.11 |
| 90% TFE | 56.8 | 15.8 | 13.4 | 13.4 | 0.100 | −1.01 | 0.85 |
| 64 mM SDS | 68.3 | 11.9 | 12.6 | 6.3 | 0.062 | −1.10 | 0.90 |
| 5 mM DPC | 71.3 | 9.4 | 7.8 | 10.1 | 0.99 | −1.96 | 0.95 |
*
For convenience of data interpretation, we added the distorted and regular components of both helical and strand secondary-structural elements together to obtain overall helical and strand structures in both Tables 1 and 2.
†
Here R1 is the ratio of the intensity of the maximum between 190 and 195 nm and the intensity of the minimum between 200 and 210 nm, and R2 is the ratio of the intensity of the minimum near 222 nm and the intensity of the minimum between 200 and 210 nm.