Table 1. Secondary structure quantitation of PhaF based in CD data.
| Sample | Method | α-Helix (%) | β-Structures (%) | Remainder (%) |
| PhaF | CDNN | 32 | 18 | 51 |
| CONTIN | 29 | 7 | 64 | |
| CDSSTR | 32 | 11 | 57 | |
| PhaF (40% TFE) | CDNN | 42 | 12 | 46 |
| CONTIN | 47 | 7 | 46 | |
| CDSSTR | 55 | 18 | 27 | |
| C-PhaF | CDNN | N.D.a | N.D. | N.D. |
| CONTIN | 1 | 4 | 95 | |
| CDSSTR | 1 | 13 | 86 | |
| C-PhaF (40% TFE) | CDNN | N.D. | N.D. | N.D. |
| CONTIN | 9 | 7 | 84 | |
| CDSSTR | 5 | 8 | 87 | |
| PhaF (whole protein) | Model | 44 | 0 | 57 |
| Model (accounting for disorder)b | 31 | 0 | 69 |
Estimations using the CDNN, CONTIN and CDSSTR procedures, and comparison with that predicted from the three-dimensional model.
a
N.D.: Not determined (poor fitting)
b
Calculations assuming that the helical-predicted stretches 13–17 and 58–91 are disordered in solution in the unligated protein (according to PONDR-FIT procedure).