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. 2012 Feb 17;7(2):e30929. doi: 10.1371/journal.pone.0030929

Table 1. Binding affinities of single mutants for MD2.

Mutant Ka (M−1 S−1) Kd (S−1) KD (M) Fold-increase
Wild-type 2.84±0.02×104 2.22±0.05×10−3 7.80±0.14×10−8 1
M41E 1.64±0.57×104 5.29±0.80×10−5 3.21±1.02×10−9 24.3
F63L 2.65±0.02×104 1.15±0.01×10−3 4.33±0.03×10−8 1.8
F63W 1.39±0.10×104 3.97±2.13×10−5 2.84±1.66×10−9 27.5
V132F 6.91±3.69×104 1.54±0.01×10−3 2.22±1.41×10−8 3.5
V134L 2.67±0.28×104 1.10±0.01×10−4 4.11±0.50×10−9 19.0
N156I 1.97±0.33×104 8.05±4.77×10−5 4.07±1.71×10−9 19.2
H159Q 2.14±1.21×103 1.00±0.44×10−5 4.30±3.23×10−9 18.1
D181E 1.91±0.10×104 9.24±1.35×10−4 4.82±0.44×10−8 1.6
S184K 7.66±0.02×103 1.41±0.02×10−3 1.83±0.04×10−7 0.4

Binding affinities (KD) of the single mutants for MD2 were measured from the association rate constants (Ka) and dissociation rate constants (Kd) using surface plasmon resonance. Fold-increase represents the ratio of binding affinities between the mutants and wild-type decoy receptor.