Table 7. Double mutant cycle analysis of the first KDL binding to wild-type and mutant MsbA trapped with ADP and vanadate.
Shown as described in Table 3.
| Temperature(K) | ΔΔG(kJ/mol) | ΔΔH(kJ/mol) | Δ(-TΔS)(kJ/mol) | ΔΔGint(kJ/mol) | ΔΔHint(kJ/mol) | Δ(-ΔTS)int(kJ/mol) | ||
|---|---|---|---|---|---|---|---|---|
| R188A | 293 | 2.7±0.1 | –28.5±3.1 | 31.2±3.1 | ||||
| 298 | 3.1±0.2 | –10.6±2.9 | 13.7±3.1 | |||||
| 303 | 3.2±0.2 | 7.3±2.9 | –4.1±2.9 | |||||
| 310 | 2.8±0.2 | 32.4±2.9 | –29.7±3.1 | |||||
| R238A | 293 | 3.2±0.2 | 104.9±6.0 | –101.7±6.0 | ||||
| 298 | 1.5±0.4 | 104.9±6.0 | –103.4±6.1 | |||||
| 303 | –0.3±0.4 | 104.9±6.0 | –105.1±6.2 | |||||
| 310 | –2.8±0.5 | 104.9±6.0 | –107.6±6.4 | |||||
| K243A | 293 | 3.7±0.1 | 74.3±5.4 | –70.7±5.3 | ||||
| 298 | 2.5±0.1 | 74.3±5.4 | –71.8±5.3 | |||||
| 303 | 1.3±0.1 | 74.3±5.4 | –73.0±5.4 | |||||
| 310 | –0.5±0.2 | 74.3±5.4 | –74.8±5.5 | |||||
| R188A | R238A | 293 | 2.2±0.2 | –32.1±3.3 | 34.2±3.4 | 3.8±0.4 | 108.5±7.0 | –104.7±7.2 |
| 298 | 2.4±0.2 | 5.3±2.9 | –2.8±2.9 | 2.2±0.5 | 89.0±6.9 | –86.9±7.1 | ||
| 303 | 2.1±0.2 | 42.6±7.5 | –40.5±7.3 | 0.8±0.5 | 69.6±9.6 | –68.7±9.8 | ||
| 310 | 0.5±0.4 | 95.0±16.5 | –94.5±16.8 | –0.5±0.6 | 42.4±17.6 | –42.8±18.1 | ||
| R188A | K243A | 293 | 4.8±0.2 | 70.5±8.7 | –65.7±8.6 | 1.6±0.2 | –24.7±10.4 | 26.3±10.3 |
| 298 | 4.0±0.1 | 60.2±4.7 | –56.2±4.5 | 1.6±0.2 | 3.5±7.2 | –1.9±7.2 | ||
| 303 | 2.6±0.1 | 51.5±1.5 | –48.8±1.3 | 1.9±0.2 | 30.1±5.8 | –28.2±5.9 | ||
| 310 | 1.9±0.1 | 33.7±5.9 | –31.8±5.9 | 0.4±0.4 | 73.0±8.1 | –72.7±8.3 | ||
| R238A | K243A | 293 | 2.3±0.1 | –13.0±14.3 | 15.3±14.2 | 4.6±0.2 | 192.2±16.2 | –187.7±16.2 |
| 298 | 2.1±0.2 | 49.9±7.3 | –47.8±7.6 | 1.9±0.4 | 129.3±10.5 | –127.4±10.9 | ||
| 303 | 0.6±0.2 | 113.4±16.3 | –112.7±16.4 | 0.4±0.5 | 65.8±17.9 | –65.4±18.2 | ||
| 310 | –3.0±0.9 | 200.5±35.8 | –203.5±36.5 | –0.4±1.0 | –21.3±36.6 | 21.1±37.5 | ||