Table 1.
Secondary structure features 1 and surface hydrophobicity of purified cruciferin and napin of B. napus at different pH levels.
| Protein | pH | α-Helix | β-Sheet | β-Turn | Random | Surface Hydrophobicity |
|---|---|---|---|---|---|---|
| (%) | (%) | (%) | (%) | (S0) 2 | ||
| Cruciferin | 3 | 10.7 ±1.0 a | 25.4 ± 3.3 a | 26.0 ± 0.7 a | 38.0 ± 3.0 a | 6666.7 ± 47.2 a |
| 7 | 7.6 ± 0.7 b | 39.2 ± 1.9 b | 20.2 ± 0.9 b | 33.1 ± 1.6 b | 346.7 ± 6.4 b | |
| 10 | 4.8 ± 0.2 c | 18.4 ± 2.2 c | 26.3 ± 0.6 a | 50.5 ± 1.1 c | 208.0 ± 1.3 c | |
| Napin | 3 | 24.1 ± 0.7 a | NA | NA | 26.3 ± 1.3 a | 1239.3 ± 19.3 a |
| 7 | 27.5 ± 1.1 b | NA | NA | 26.9 ± 1.4 a | 103.6 ± 3.9 b | |
| 10 | 27.2 ± 0.7 a,b | NA | NA | 25.4 ± 0.6 a | 150.4 ± 1.6 c |
1 From far-UV CD data; Means ± Standard error (SE); 2 S0 from ANS fluorescence probe; Means followed by same superscript within the same column and same protein type are not significant (p > 0.05).