TABLE 2.
Predicted changes in secondary structure of recombinant NR7 and rP1 during thermal denaturation
Changes were calculated by measuring the far UV CD spectra from 260–185 nm during heating and using the deconvolution algorithm CDSSTR (51–56). The protein reference set was SDP42.
| Secondary structure content | 25 °C | 40 °C | 45 °C | 50 °C | 52 °C | 54 °C | 56 °C | 58 °C | 60 °C | 65 °C | 70 °C |
|---|---|---|---|---|---|---|---|---|---|---|---|
| rP1 | |||||||||||
| α-Helical content | 53% | 53% | 51% | 49% | 42% | 37% | 24% | 20% | 17% | 8% | 6% |
| β-Sheet content | 20% | 20% | 16% | 14% | 16% | 14% | 19% | 17% | 18% | 23% | 29% |
| β-Turn content | 12% | 11% | 14% | 17% | 19% | 18% | 21% | 18% | 17% | 16% | 19% |
| Unordered content | 15% | 16% | 19% | 20% | 23% | 31% | 36% | 45% | 48% | 53% | 46% |
| NR7 | |||||||||||
| α-Helical content | 50% | 50% | 50% | 43% | 36% | 24% | 20% | 15% | 8% | 7% | 5% |
| β-Sheet content | 23% | 24% | 17% | 15% | 17% | 17% | 18% | 22% | 24% | 25% | 31% |
| β-Turn content | 14% | 12% | 15% | 17% | 18% | 18% | 19% | 19% | 17% | 17% | 18% |
| Unordered content | 13% | 14% | 18% | 25% | 29% | 41% | 43% | 44% | 51% | 51% | 46% |