Table 2.
Conformation changes of EPS proteins from R. faecalis RLD-53 at different concentration of L-cysteine
| Secondary structures | Wavenumber (cm-1) |
L-cysteine (g/l) |
|||
|---|---|---|---|---|---|
| 0.0 | 0.5 | 1.0 | 1.5 | ||
| Aggregated strands (%) |
1625-1610 |
1.55 |
1.21 |
2.51 |
2.01 |
| β-Sheet (%) |
1640-1630 |
11.33 |
14.73 |
21.09 |
25.31 |
| Random coil (%) |
1645-1640 |
37.50 |
27.30 |
3.28 |
5.52 |
| α-Helix (%) |
1657-1648 |
16.96 |
25.52 |
49.40 |
31.03 |
| 3-Turn helix (%) |
1666-1659 |
20.13 |
27.63 |
21.35 |
34.54 |
| Antiparallel β-sheet/ aggregated strands (%) | 1680-1695 | 12.53 | 3.62 | 2.38 | 1.59 |