Table 1. Secondary structure content of various FlhBC. Secondary structure content was calculated from the CD spectra using a multilinear regression [36].
| Protein | α-helix, % | β-structure, % | β-turn, % | random coil, % |
| AquFlhBC347 | 28.5±0.1 | 28.7±0.1 | 5.2±2.9 | 37±1.8 |
| AquFlhBC V341 f.-s. | 31.3±1.5 | 25.3±0.7 | 6.1±0.5 | 37.4±2.8 |
| AquFlhBC347 ΔKG(288–289) | 17.3±1.3 | 30.4±0.3 | 6.1±0.01 | 46.4±1.1 |
| AquFlhBC347 F330L | 32±3.1 | 26.1±1.3 | 4.45±1.1 | 37.5±0.01 |
| AquFlhBC357 V259E | 27.3±1.3 | 25.8±1.6 | 6.5±0.7 | 40.4±0.4 |
| AquFlhBC347 V307G | 28.4±1.8 | 27.7±1.0 | 4.6±0.3 | 39.4±0.4 |
| SalFlhBC | 40.8±0.7 | 14.4±0.6 | 9.9±1.5 | 34.9±0.2 |