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. 2011 Nov 10;287(1):347–356. doi: 10.1074/jbc.M111.256271

TABLE 1.

Apparent dissociation constant (Kd) values for the interaction of TCP proteins and their respective mutants with C20 and C16

Binding curves were fitted to the Hill equation with a Hill number of 2, assuming that dimer formation is required for DNA binding. ΔKd indicates the S.D. of three independent experiments. Values indicate concentration of TCP monomers. The root mean square deviation (r.m.s.d.) errors and correlation coefficients (r2) of the fits to the experimental data are also indicated.

Protein C20
C16
Kd ΔKd r.s.m.d. r2 Kd ΔKd r.s.m.d. r2
nm nm % nm nm %
TCP16 81.2 7.2 12.3 0.980 49.2 2.2 3.2 0.996
D11G-TCP16 238.6 8.4 10.7 0.962 239.3 25.1 10.9 0.961
TCP20 122.0 5.6 9.7 0.956 169.1 13.8 14.5 0.892
G11D-TCP20 138.4 1.0 9.6 0.970 68.4 5.1 11.6 0.939
TCP4 157.4 13.9 9.8 0.932 99.1 7.1 10.6 0.944
D15G-TCP4 162.6 23.1 6.1 0.983 162.6 1.5 7.2 0.979