Table 2. Properties of expressed peptides.
| Domain | Size | [Θ222]MRW degrees cm2 dmol−1 residue−1 | α-helixc % | α-helixd % | Dimer formation | ||
|---|---|---|---|---|---|---|---|
| Residuesa | Calculated (kDa) | SDS-PAGE (kDa)b | |||||
| ABD | 236 | 27.4 | 26 | 15,053 | 46.3 | 47.5 | no |
| ROD | 258 | 30.4 | 30 | 18,060 | 54.0 | 81.0 | yes |
| EF | 147 | 16.9 | 17 | 12,919 | 40.8 | 61.2 | no |
| EF-hise | 156 | 18.0 | 17 | nd | nd | nd | no |
| ABD-ROD | 485 | 56.7 | 57 | 20,807 | 61.0 | 66.6 | yes |
| ROD-EF | 396 | 46.3 | 47 | 24,351 | 70.1 | 78.0 | yes |
Notes.
a
Includes two N-terminal residues from the cloning vector, except for EF-his that includes 3 N-terminal residues and 6 histidines at the C-terminal.
b
Estimated from Coomassie blue-stained polyacrylamide gels.
c
The α-helical content estimated as: (−[Θ222]MRW + 3,000)∕39,000 (Morrow et al., 2000).
d
MLRC (Guermeur et al., 1999) at Pôle Bioinformatique Lyonnaise was used to predict the secondary structure.
e
EF-his was obtained from plasmid pGST-TEV-SP-EF.
- nd
- Not determined