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. Author manuscript; available in PMC: 2010 Aug 20.
Published in final edited form as: Methods Enzymol. 2004;384:212–232. doi: 10.1016/S0076-6879(04)84013-8

Table 2.

Equilibrium Constants for binding of PKR dsRBD to a 20-mer RNA as determined by sedimentation equilibrium.

Model ln K1a ln K2a ln K3a ln kb RMS X10−3c
Unconstrainedd 18.32 [17.21,19.48] 15.38 [14.43,16.94] 14.07 [13.54,14.47] - 4.37
N=14, Δ=3e 17.96 16.37 13.71 16.01 [15.77,16.23] 4.48
N=12, Δ=4e 18.51 16.82 13.60 16.31 [16.07, 16.58] 4.48
a

Natural logarithm of the macroscopic binding constant. The values in brackets represent the 95% joint confidence intervals.

b

Natural logarithm of the intrinsic binding constant. The values in brackets represent the 95% joint confidence intervals.

c

Root mean square deviation of the fit in absorbance units (OD).

d

Independent binding of three ligands. The natural logarithms of the macroscopic binding constants are the fitted parameters.

e

Finite lattice models. The natural logarithms of the intrinsic binding constants are the fitted parameters. The macroscopic binding constants are calculated using coefficients determined by equation 11.