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. 2013 Feb 21;288(15):10766–10778. doi: 10.1074/jbc.M113.455592

TABLE 1.

Summary of biophysical constants of protein-protein interactions

N.D. indicates not detected.

Interaction ITC
SPR
ΔG ΔH TΔS Stoichiometry Kd kon koff Kd χ2 (U value)
kcal/mol kcal/mol kcal/mol m1 s1 s1 nm
SinI-SinR −11.9 −8.36 ± 0.16 −3.58a 1.27 ± 0.01 ≤10 nm 2.73 ± 0.01 × 104 5 ± 0.06 × 10−5 1.83 0.12 (5)
SlrA-SinR −10.9 −7.89 ± 0.44 −2.97a 0.89 ± 0.02 ≤10 nm 2.16 ± 0.01 × 104 2.3 ± 0.006 × 10−4 10.6 40.8 (1)
SlrR-SinR N.D. N.D. N.D. N.D. N.D. 4.85 ± 0.03 × 103 2.3 ± 0.015 × 10−4 47.5 0.10 (NA)
SinR-Inverted repeat DNA −8.77 4.33 ± 0.12 −13.12 2.38 ± 0.05 360 ± 122 nm 1 × 105b 2 × 10−2b 270 ± 50 N.D.
SinR-Single site DNA −6.68 −5.78 ± 0.11 0.90 1.07 ± 0.01 12.5 ± 1.2 μm N.D. N.D. N.D. N.D.
SinR-Tandem site DNA −6.18 1.66 ± 0.13 −7.84 ∼2 30 ± 7 μm N.D. N.D. N.D. N.D.

a Kd measured by SPR was used for fitting ITC data to obtain ΔS.

b Values estimated by simulation software from data of Colledge et al. (11).