Table 8. Double mutant cycle analysis of the second 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±0.2 | –42.2±2.4 | 44.9±2.6 | ||||
| 298 | 3.2±0.2 | –21.6±3.3 | 24.8±3.4 | |||||
| 303 | 3.5±0.4 | –0.9±4.4 | 4.3±4.5 | |||||
| 310 | 3.2±0.4 | 28.0±5.9 | –24.8±6.1 | |||||
| R238A | 293 | 4.4±0.5 | 102.7±10.8 | –98.2±10.8 | ||||
| 298 | 2.7±0.5 | 102.7±10.8 | –100.0±11.0 | |||||
| 303 | 1.0±0.5 | 102.7±10.8 | –101.6±11.1 | |||||
| 310 | –1.3±0.7 | 102.7±10.8 | –104.0±11.4 | |||||
| K243A | 293 | 4.2±0.4 | 76.7±6.9 | –72.5±6.6 | ||||
| 298 | 2.9±0.2 | 76.7±6.9 | –73.8±6.7 | |||||
| 303 | 1.7±0.2 | 76.7±6.9 | –75.0±6.9 | |||||
| 310 | –0.1±0.4 | 76.7±6.9 | –76.8±7.1 | |||||
| R188A | R238A | 293 | 3.5±0.2 | –43.2±30.4 | 46.7±30.3 | 3.6±0.4 | 103.7±32.3 | –100.0±32.2 |
| 298 | 3.9±0.5 | –3.1±13.7 | 7.0±14.2 | 2.0±0.6 | 84.2±17.8 | –82.3±18.2 | ||
| 303 | 3.6±0.4 | 37.5±4.9 | –33.9±4.8 | 0.9±0.6 | 64.3±12.6 | –63.3±13.0 | ||
| 310 | 2.2±0.2 | 92.7±25.8 | –90.5±25.8 | –0.3±0.9 | 38.0±28.7 | –38.3±28.9 | ||
| R188A | K243A | 293 | 6.3±0.7 | 100.4±44.8 | –94.1±44.1 | 0.6±0.7 | –65.9±45.4 | 66.5±44.7 |
| 298 | 4.9±0.2 | 79.7±25.2 | –74.8±25.2 | 1.2±0.2 | –24.6±26.3 | 25.8±26.3 | ||
| 303 | 3.6±0.4 | 59.5±5.8 | –55.9±5.6 | 1.5±0.4 | 16.3±9.9 | –14.7±9.9 | ||
| 310 | 2.7±0.2 | 29.4±22.9 | –26.7±22.9 | 0.4±0.4 | 75.3±24.6 | –74.9±24.7 | ||
| R238A | K243A | 293 | 3.2±0.2 | –28.5±2.2 | 31.7±2.2 | 5.4±0.5 | 207.9±13.0 | –202.4±12.9 |
| 298 | 3.4±0.2 | 21.1±2.2 | –17.7±2.3 | 2.2±0.4 | 158.3±13.0 | –156.1±13.1 | ||
| 303 | 2.5±0.2 | 71.2±5.4 | –68.7±5.5 | 0.2±0.5 | 108.2±13.8 | –107.9±14.2 | ||
| 310 | 0.2±0.4 | 139.4±10.5 | –139.2±10.8 | –1.6±0.9 | 40.0±16.5 | –41.6±17.3 | ||