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. 2013 Apr 22;591(Pt 13):3289–3308. doi: 10.1113/jphysiol.2013.252189

Table 4.

Mean rate constants, equilibrium constants and coefficients of variations from the fit of flip mechanisms with different numbers of binding sites

Units Flip, 3 binding sites (Scheme 3) Flip, 4 binding sites Flip, 5 binding sites (Scheme 4)
α1 s−1 2840 ± 30%
β1 s−1 1230 ± 4%
α2 s−1 498 ± 16% 2690 ± 27%
β2 s−1 18,800 ± 14% 1220 ± 7%
α3 s−1 2370 ± 28% 496 ± 14% 2520 ± 23%
β3 s−1 154,000 ± 15% 19,600 ± 13% 1260 ± 7%
α4 s−1 2030 ± 24% 497 ± 13%
β4 s−1 149,000 ± 16% 20,700 ± 10%
α5 s−1 1870 ± 22%
β5 s−1 147,000 ± 16%
γ1 s−1 1830 ± 23%
δ1 s−1 91 ± 20%
γ2 s−1 6180 ± 1% 1950 ± 13%
δ2 s−1 4280 ± 17% 223 ± 23%
γ3 s−1 2120 ± 27% 5900 ± 5% 2220 ± 13%
δ3 s−1 17,500 ± 10% 5060 ± 18% 419 ± 31%
γ4 s−1 2490 ± 26% 5800 ± 7%
δ4 s−1 14,500 ± 8% 5820 ± 22%
γ5 s−1 2550 ± 27%
δ5 s−1 12,700 ± 5%
k- s−1 241 ± 1% 236 ± 15% 222 ± 23%
k+ m−1 s−1 (7.32 × 104) ± 9% (1.60 × 105) ± 6% (2.45 × 105) ± 14%
kf- s−1 4480 ± 9% 5270 ± 13% 5920 ± 16%
kf+ m−1 s−1 (9.88 × 106) ± 29% (9.73 × 106) ± 24% (9.73 × 106) ± 21%
E111 0.52 ± 30%
E222 41 ± 24% 1 ± 28%
E333 70 ± 14% 42 ± 22% 1 ± 24%
E444 77 ± 11% 44 ± 19%
E555 80 ± 8%
F1=δ1/γ1 0.05 ± 31%
F2=δ2/γ2 0.69 ± 16% 0.11 ± 19%
F3=δ3/γ3 11 ± 45% 1 ± 24% 0.18 ± 20%
F4=δ4/γ4 7 ± 42% 1 ± 29%
F5=δ5/γ5 6 ± 42%
KR=k/k+ μm 3350 ± 11% 1460 ± 10% 885 ± 9%
KF=kf−/kf+ μm 263 ± 25% 196 ± 19% 159 ± 15%
EC50 μm 320 ± 8% 300 ± 5% 275 ± 7%
nH 2.2 ± 5% 2.7 ± 4% 3.1 ± 3%

The fits constrain the binding and unbinding rates to be the same, regardless of the number of molecules bound, in any conformation. The equilibrium constants, E, F and K, and open probability curve EC50 and the Hill slope, nH, were calculated from the rate constants for each set and then averaged. Values are means ± coefficient of variation (i.e. SD of the mean expressed as a percentage of the mean).