TABLE 2.
Analysis of protein-protein interactions between YnjE and different protein partners by SPR measurements
| Immobilized proteina | RUb | Protein partnerc | KDd | c2 |
|---|---|---|---|---|
| μm | ||||
| YnjEΔ1–21 | 190 | BSA | NDe | —f |
| YnjEΔ1–21 | 190 | IscS | 1.36 | 1.89 |
| YnjEΔ1–21 | 190 | SufS | ND | — |
| YnjEΔ1–21 | 190 | CsdA | ND | — |
| YnjEΔ1–21 | 190 | MoeB | 0.58 | 0.91 |
| YnjEΔ1–21 | 190 | MoaE | 10.6 | 0.31 |
| YnjEΔ1–21 | 190 | MoaD | ND | — |
| MoaD | 183 | BSA | ND | — |
| MoaD | 183 | YnjEΔ1-21 | 1.49 | 0.38 |
| MoaD | 183 | MoaE | 0.29 | 2.00 |
| MoaD | 183 | IscS | 0.54 | 0.74 |
| MoaD | 183 | SufS | ND | — |
| MoaD | 183 | CsdA | ND | — |
| MoeB | 198 | MoaD | 8.71 | 0.27 |
| MoeB | 198 | IscS | 0.16 | 0.46 |
| MoeB | 198 | BSA | ND | — |
a Proteins were immobilized via surface thiol coupling (see “Experimental Procedures”).
b Resonance units.
c Proteins were injected using the KINJECT protocol, injecting samples in a concentration range of 0.8–25 μm. Cells were regenerated by injection of 20 mm HCl.
d KD values were obtained by global fitting procedures for a 1:1 binding.
e ND, no binding detectable.
f —, not calculated.