Table 1.
FLIPPi affinity mutants
| Sensor | Sequence | Kd (M)a | ΔRmaxa,b | Hill coefficient | Dynamic rangec |
|---|---|---|---|---|---|
| FLIPPi-260n | Wild-type | 2.6 × 10−7 | −0.13 | 1.03 | 25–1200 nM |
| FLIPPi-770n | S161A | 7.7 × 10−7 | −1.07 | 1.03 | 80–5600 nM |
| FLIPPi-4µ | T163A | 3.9 × 10−6 | −1.34 | 1.02 | 0.4–25 µM |
| FLIPPi-5µ | S52A | 5.1 × 10−6 | −1.33 | 1.03 | 0.5–34 µM |
| FLIPPi-200µ | G162A | 2.1 × 10−4 | −1.13 | 1.00 | 25–1600 µM |
| FLIPPi-30m | T22A | 3.3 × 10−2 | −1.03 | 1.03 | 3–170 mM |
Binding constants determined in vitro.
a
R2 for the fit exceeded 0.98 in all analyses.
b
ΔRmax, in vitro maximum change in ratio between ligand-free and ligand-saturated sensor.
c
Range between 10% and 90% saturation of the sensor (the effective quantification range).