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. Author manuscript; available in PMC: 2014 Feb 7.
Published in final edited form as: Mol Cell. 2012 Dec 27;49(3):571–582. doi: 10.1016/j.molcel.2012.11.026

Table 1.

Summary of thermodynamic and curve fitting parameters for ITC assays using recombinant PHF1 or PHF19 Tudor domain proteins and various histone peptides. See also Figures S1L-S and S2G.

Protein Peptide ΔH(cal/mol) ΔS
(cal/mol/deg)
Ka(M-1) N Chi2/
DoF
Kd (µM)
PHF1Tudor, wt H3(28–43)K36me3 −5626 ± 108 4.45 2.38E5 ± 1.91E4 0.79 ± 0.01 5415 4.2 ± 0.3
PHF1Tudor, wt H3(28–43)K36me2 −3994 ± 261 7.26 5.18E4 ± 6.79E3 0.94 ± 0.04 4338 19.3 ± 2.5
PHF1Tudor, wt H3(28–43)K36me1 −817 ± 342 17.3 2.63E4 ± 1.12E4 0.70 ± 0.23 658.3 38.0 ± 16.1
PHF1Tudor, wt H3(28–43)K36me0 -- -- -- -- -- N.D
PHF1Tudor, wt H3(19–35)K27me3 −5141 ± 469 −1.21 5.93E3 ± 486 1.03 ± 0.07 347.7 168 ± 13.8
PHF1Tudor, wt H3(1–15)K9me3 −817 ± 343 17.3 2.63E4 ± 1.12E4 0.70 ± 0.23 658.3 38.0 ± 16.2
PHF1Tudor, W41A H3(28–43)K36me3 −1355 ± 457 15.8 3.32E4 ± 1.20E4 0.68 ± 0.18 1456 30.1 ± 10.9
PHF1Tudor, Y47A H3(28–43)K36me3 -- -- -- -- -- N.D.
PHF1Tudor, F65A H3(28–43)K36me3 -- -- -- -- -- N.D.
PHF1Tudor, F71A H3(28–43)K36me3 -- -- -- -- -- N.D.
PHF1Tudor, E66K H3(28–43)K36me3 −6471 ± 229 −1.94 4.39E4 ± 3.76E3 0.60 ± 0.02 5055 22.8 ± 2.0
PHF19Tudor, wt H3(27–46)K36me3 −6610 ± 267 0.466 1.60E5 ± 1.65E4 0.58 ± 0.02 7436 6.2 ± 0.6
PHF19Tudor, wt H3(27–46)K36me1 -- -- -- -- -- N.D.
PHF19Tudor, Y56A H3(27–46)K36me3 -- -- -- -- -- N.D.

wt, wildtype; N.D, not determined.