. Author manuscript; available in PMC: 2018 Dec 12.

Published in final edited form as: Biochemistry. 2017 Nov 22;56(49):6503–6514. doi: 10.1021/acs.biochem.7b00836

Table 1.

Measured binding affinities between engineered IpaD π-helix mutants and the bile salt deoxycholate

IpaD Mutant	K_d (μM) ± SD^a
Wild-type IpaD	9.3 ± 1.8
D144A	10.5 ± 2.5
N146A	10.9 ± 0.2
Y149A	10.8 ± 0.3
D144A/N146A	9.7 ± 1.7
D144A/Y149A	10.7 ± 1.5
N146A/Y149A	9.9 ± 2.3
D144A/N146A/Y149A	8.3 ± 2.2

Apparent K_d values between IpaD and fluorescein-DOC reported as the mean ± standard deviation resulting from three independent analyses. There is no statistical difference among the means (one-way ANOVA (F(7,16) = 0.803, p = 0.597)).