. 2014 Nov 20;42(22):13861–13872. doi: 10.1093/nar/gku1208

Table 3. Binding affinities of Mtr4 and mutants on a poly(A) substrate as determined by fluorescence anisotropy^a.

	K_d (μM)
Mtr4^WT	2.8 ± 0.9
Mtr4^archless	4.5 ± 0.6
Mtr4^R1030A	2.6 ± 1.0
Mtr4^E1033A	2.0 ± 0.6
Mtr4^{R1030A-archless}	> 10
Mtr4^{E1033A-archless}	4.8 ± 0.6

Binding affinities > 10 μM were not quantified by anisotropy. Data presented here represent averages from three independent experiments; error bars represent SD.

^aMethods and equations used to derive kinetic constants are found in the ‘Materials and Methods’ section.

Table 3. Binding affinities of Mtr4 and mutants on a poly(A) substrate as determined by fluorescence anisotropya.

Table 3. Binding affinities of Mtr4 and mutants on a poly(A) substrate as determined by fluorescence anisotropy^a.