Table 1:
Analytical ultracentrifugation analysis of DIP and Dpr homodimers
| Protein | Monomer MW from Mass Spectrometry (kDa) |
Apparent MW in AUC (kDa) |
Oligomeric state |
KDdimerization (μM) |
RMSDs |
|---|---|---|---|---|---|
| Dprs | |||||
| Dpr8 | 29.2 | 43.0 ± 0.05 | Dimer | 39.0 ± 0.2 | 0.00772 ± 0.00034 |
| Dpr12 | 28.9 | 35.0 ± 0.75 | Dimer | 71.3 ± 7.6 | 0.00598 ± 0.00004 |
| Dpr21 | 28.9 | 39.9 ± 0.93 | Dimer | 49.1 ± 4.0 | 0.00767 ± 0.00057 |
| DIPs | |||||
| DIP-α | 36.4 | 54.0 ± 0.19 | Dimer | 23.9 ± 0.03 | 0.00746 ± 0.00055 |
| DIP-ζ | 40.9 | 59.0 ± 0.47 | Dimer | 22.2 ± 2.1 | 0.00759 ± 0.00102 |
| DIP-η | 40.5 | 56.2 ± 0.05 | Dimer | 35.4 ± 0.4 | 0.00848 ± 0.00030 |
| DIP-θ | 44.0 | ND | Dimer* | ND | ND |
MW, Molecular Weight. ND, Not Determined. RMSDs represent the error of the global fit.
AUC data are presented as the mean of two independent measurements, ± the difference of each of these from the mean
DIP-θ was determined to be a dimer by SEC-MALS (See Figure S4B)