A/Perth/16/2009 (H3N2), = 28 nM Kd A/Victoria/361/2011 (H3N2), = 35 nM Kd A/duck/Czechoslovakia/1956 (H4N6), = 390 nM Kd A/chicken/Netherlands/219/2003 (H7N7), = 190 nM Kd These data were fit with a 2:1 binding model, yielding apparent = 130 nM and = 250 Kd1 Kd2 nM (although and differ for the two binding processes). As these two binding processes kon koff have similar affinities, we report the affinity as the average of and ~190 nM, in Figure Kd1 Kd2, 2. A/chicken/Germany/N/1949 (H10N7), = 0.7 nM Kd A/mallard/Astrakhan/263/1982 (H14N5), = 480 nM Kd These data were fit with a 2:1 binding model, yielding apparent = 500 nM and = 460 Kd1 Kd2 nM (although and differ for the two binding processes). As these two binding processes kon koff have similar affinities, we report the affinity as the average of and ~480 nM, in Figure Kd1 Kd2, 2. A/shearwater/West Australia/2576/1979 (H15N9), = 350 nM Kd These data were fit with a 2:1 binding model, yielding apparent = 350 nM and = 11 Kd1 Kd2 nM. The dominant binding process (accounting for the majority of the shift in observed wavelength) corresponds to the lower affinity process (Kd1 = 350 nM). The higher affinity process may reflect a non-specific interaction. Therefore, we report the affinity for this interaction as 350 nM in Figure 2.
A/Perth/16/2009 (H3N2), Kd = 28 nM A/Victoria/361/2011 (H3N2), Kd = 35 nM A/duck/Czechoslovakia/1956 (H4N6), Kd = 390 nM A/chicken/Netherlands/219/2003 (H7N7), Kd = 190 nM These data were fit with a 2:1 binding model, yielding apparent Kd1 = 130 nM and Kd2 = 250 nM (although kon and koff differ for the two binding processes). As these two binding processes have similar affinities, we report the affinity as the average of Kd1 and Kd2, ~190 nM, in Figure 2. A/chicken/Germany/N/1949 (H10N7), Kd = 0.7 nM A/mallard/Astrakhan/263/1982 (H14N5), Kd = 480 nM These data were fit with a 2:1 binding model, yielding apparent Kd1 = 500 nM and Kd2 = 460 nM (although kon and koff differ for the two binding processes). As these two binding processes have similar affinities, we report the affinity as the average of Kd1 and Kd2, ~480 nM, in Figure 2. A/shearwater/West Australia/2576/1979 (H15N9), Kd = 350 nM These data were fit with a 2:1 binding model, yielding apparent Kd1 = 350 nM and Kd2 = 11 nM. The dominant binding process (accounting for the majority of the shift in observed wavelength) corresponds to the lower affinity process (Kd1 = 350 nM). The higher affinity process may reflect a non-specific interaction. Therefore, we report the affinity for this interaction as 350 nM in Figure 2.
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