Table 1. Rate Constants for OBS Peptide Binding to OmpFa.
OBS12–18 from the periplasmic side | OBS254–63 from the extracellular side | |
---|---|---|
k1 (106 M–1 s–1) | 9.6 ± 0.60 | 4.0 ± 0.60 |
k2 (106 M–1 s–1) | 6.1 ± 0.42 | 2.2 ± 0.64 |
k3 (106 M–1 s–1) | 3.2 ± 0.25 | 0.97 ± 0.50b |
k–1 (s–1) | 43 ± 1.5 | 1.3 ± 0.10 × 104 |
k–2 (s–1) | 78 ± 3.9 | 2.5 ± 0.34 × 104 |
k–3 (s–1) | 111 ± 6.6 | 3.2 ± 0.47 × 104 |
Kd (μM)c | 13 ± 1.0 | 11 ± 2.0 × 103 |
The values are estimates at 0 mV obtained by extrapolation (Figure 1). Each rate constant and its standard deviation were determined from at least three independent experiments. Each experiment generated thousands of reversible binding events unless otherwise stated.
Due to fewer events in which all three subunits were occluded (<100) in the case of OBS254–63, the error in k3 is relatively large compared to those for the other rate constants.
Kd values for a single OmpF subunit were statistically corrected by using the mean association and dissociation rate constants.