Resolution:
## Figure 6.
Simultaneously fitting binding data from several different concentrations of α4β2
nAChR identifies low-affinity specific binding. A. The one site model_{total }and two sites model_{total }with [^{3}H]EB_{max }= 100 nM were fitted to noisy binding data with R1T = 0.065, 0.13, and 0.39 nM and
α = 0. SD for noise at the R1T values was 0.002, 0.004, and 0.012, respectively (maximum
S/N ratio≃36). The two sites model_{total }shows a significantly better fit (p = 4 × 10^{-7}). B. The y-axis shows p values for comparisons of one site model_{total }and two sites model_{total }from various [^{3}H]EB_{max }values. The fitted data sets are analogous to the data sets shown in A; p-values from 5 data sets appear at each x-coordinate. Solid lines connect averages of log(p) values. The CIs of estimates of K_{d1 }(9.2-18.5 pM; mean = 13.0 pM) and K_{d2 }(1.0-1400 nM; mean = 38 nM) and R2T (0.015-0.66; mean = 0.34) (n = 5 for each CI) include true values.
Person and Wells |