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. 2021 Jul 9;478(13):2571–2587. doi: 10.1042/BCJ20210295

Table 1. Thermodynamic parameters of the interaction of Δ21TgCEN1 and its N- and C-terminal domains with P17-XPC in the presence of 5 mM CaCl2 or 5 mM EGTA at 25°C.

Buffer condition n Kd (nM) ΔH (kJ mol−1) −TΔS (kJ mol−1)
Δ21TgCEN1 + P17-XPC CaCl2 n1 = 0.7 ± 0.1 1.3 ± 0.3 −99.7 ± 5.3 48.6 ± 5.8
n2 = 0.8 ± 0.1 4102 ± 914 −50.8 ± 11.3 25.7 ± 11.5
EGTA 0.9 ± 0.1 59.1 ± 11.8 −131.7 ± 1.6 89.9 ± 1.9
Δ21N-TgCEN1 + P17-XPC CaCl2 0.7 ± 0.1 396.3 ± 60.9 −74.25 ± 4.3 37.4 ± 3.9
EGTA - - - -
C-TgCEN1 + P17-XPC CaCl2 0.8 ± 0.1 6.7 ± 1.1 −95.7 ± 9.9 48.8 ± 10.2
EGTA 0.8 ± 0.1 50.1 ± 9.7 −118.7 ± 2.9 76.5 ± 3.1

The reported parameters are the mean ± standard error of the mean (SEM) of at least three independent titrations using two different protein preparations.