Table 1.
The temperature at which oligomers (trimers/dimers) dissociate into monomers, as well as the oligomeric state of the wild type and mutants, which are as designed. Wild type and mutant proteins were subjected to temperature increases of 2°C from 20 to 90°C. The dissociation temperature was measured through SDS-PAGE separation. ΔT is the difference in the dissociation temperature of the respective mutant OmpF and the wild type: ΔT = Tmutant − Twildtype
| Mutant | Dissociation Temperature (°C) | ΔT (°C) | Oligomerization State |
|---|---|---|---|
| Wild Type | 73(±1) | NA | Trimer |
| G19W | 47(±2) | −26 | Trimer |
| R100L | 52(±2) | −21 | Trimer |
| G135W | 52(±2) | −21 | Trimer |
| N141W | 67(±2) | −6 | Trimer |
| R100L/G135W | 44(±1) | −29 | Dimer |
| R100L/G19W | NA | NA | Monomer |
| G57A/G59A | 63(±1) | −10 | Trimer |
| G57S/G59S | 61(±1) | −12 | Trimer |
| G57I/G59L | NA | NA | Monomer |