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. 2013 Nov 27;42(4):2736–2749. doi: 10.1093/nar/gkt1171

Table 1.

Equilibrium dissociation constants (Kd) for Trp mutants to A15 and U6

A15
U6
E. coli Hfq
WT Hfq S 1.4 nM ± 0.9 a,b Fold changec 766.0 nM ± 73.7 Fold change
F11W 7.1 nM ± 0.6 5.0 502.7 nM ± 55.5 0.7
R17W 3.7 nM ± 1.5 2.6 1.6 µM ± 0.08 2.1
Y25W 258.2 nM ± 32.7 184.4 836.8 nM ± 62.5 1.1
K31W 1.4 nM ± 0.5 1.0 1123.3 ± 73.0 1.5
Q33W 15.9 nM ± 3.6 11.4 404.7 nM ± 182.4 0.5
F39W 0.59 nM ± 0.35 0.4 2.0 µM ± 0.4 2.6
F42W 0.28 nM ± 0.09 0.2 4.8 µM ± 782.5 6.2
G77W 2.9 nM ± 1.7 2.1 379.9 nM ± 93.2 0.5
Y83W 7.4 nM ± 2.8 5.3 777.9 nM ± 254.1 1.0
Q95W 2.6 nM ± 1.1 1.9 848.3 nM ± 289.4 1.1
S. aureus Hfq
WT Hfq 4.2 nM ± 0.5 d 69.8 nM ± 7.0 d
F25W 11.3 µM ± 5.0 2700 41.9 nM ± 25.1 0.6
Q31W 1.6 µM ± 0.08 386.7 114 nM ± 23.2 1.6

aEach value is the average of three individual experiments and the standard deviations.

bTaken from (39).

cFold change is the ratio of the Kd of the mutant Hfq divided by the Kd of the WT Hfq.

dTaken from (41). Values listed in bold are all fold increases above 10.0.