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. 2006 Dec;18(12):3647–3655. doi: 10.1105/tpc.106.047316

Table 2.

Thermodynamic Parameters of Association for At-OASS and C10 Peptide

Kd (nM) Inline graphic ΔH −TΔS ΔG
Wild type 5.6 ± 2.0 (37 ± 12) 1.8 ± 0.8 × 108 (2.7 ± 0.9 × 107) −9.7 ± 0.3 (−1.3 ± 0.4) −1.6 (−8.8) −11.3 ± 0.3 (−10.1 ± 0.2)
T74S 100 ± 11 9.4 ± 0.1 × 106 −5.8 ± 0.17 −3.6 −9.5 ± 0.08
S75A 40 ± 3 2.5 ± 0.2 × 107 −9.2 ± 0.12 −0.8 −10.0 ± 0.05
S75T 1471 ± 50 6.8 ± 0.5 × 105 −5.9 ± 0.3 −2.0 −7.8 ± 0.08
Q147A 56 ± 13 1.8 ± 0.3 × 107 −8.8 ± 0.3 −0.9 −9.9 ± 0.08

Values of ΔH, TΔS, and ΔG are in kcal mol−1. Wild-type data were fit to the equation describing a two-site binding, with the parameters for the second binding site shown in parentheses. Mutant data were fit to the equation describing a single-site binding model.