Table 1.
Structural properties of nesprin-1α fragments calculated from the CD spectra in Figure 2, and protein size measured by DLS at 25°C unless otherwise noted.
| Circular Dichroism analysis | DLS | |||||
|---|---|---|---|---|---|---|
| Protein fragments | %α-helix | %β-sheet | %Turn | θ222/θ208 | Size(nm) | monomer (nm) |
| SLR2-5 | 74.5±4.5 | 2.4±0.7 | 7.7±2.0 | 0.95 | 35.4±5.4 | |
| SLR2-7 | 88.2±4.1 | 0.4±0.2 | 0.9±0.5 | 0.91 | 99.0±14.9 | 57.4±13.1 (58°C) |
| SLR5-7 | 83.1±3.9 | 2.7±0.4 | 3.8±2.2 | 0.88 | 36.1±6.1 | |
| SLR2-7ΔAD | 78.4±5.0 | 1.6±0.3 | 4.7±1.3 | 0.96 | 76.1±7.8 | 53.6±4.45 (42°C) |
| AD | 32.7±4.3 | 18.3±2.1 | 20.2±1.3 | NTa | NT | NT |
a
NT indicates not tested. The θ222/θ208 ratio is useful for high helix proteins, not for AD alone. Similarly, isolated AD is in its disordered state, so size analysis is not appropriate.