Rate and Equilibrium Constants of Loop 5 Deletion Mutants Activated by ACh
Construct . | k+ . | k−1 . | Kd . | β2 . | α2 . | L2 . |
---|---|---|---|---|---|---|
μM−1 s−1 | s−1 | s−1 | s−1 | |||
wt | 167 ± 2 | 24,745 ± 257 | 148 | 50,000 | 2,100 | 23.8 |
Del 97 | 42 ± 4 | 15,099 ± 1,185 | 359 | 3,928 ± 132 | 6,704 ± 744 | 0.59 |
Del 97-98 | 63 ± 2 | 5,008 ± 135 | 79 | 7,715 ± 174 | 4,045 ± 131 | 1.91 |
Construct . | k+ . | k−1 . | Kd . | β2 . | α2 . | L2 . |
---|---|---|---|---|---|---|
μM−1 s−1 | s−1 | s−1 | s−1 | |||
wt | 167 ± 2 | 24,745 ± 257 | 148 | 50,000 | 2,100 | 23.8 |
Del 97 | 42 ± 4 | 15,099 ± 1,185 | 359 | 3,928 ± 132 | 6,704 ± 744 | 0.59 |
Del 97-98 | 63 ± 2 | 5,008 ± 135 | 79 | 7,715 ± 174 | 4,045 ± 131 | 1.91 |
The binding and gating rate constants were estimated by jointly fitting interval durations elicited by different concentrations of ACh, using Scheme I (see Fig. 11). Kd was calculated as the ratio k−/k+. Wild type values are from (Salamone et al., 1999).