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. Author manuscript; available in PMC: 2021 Nov 12.
Published in final edited form as: J Mol Biol. 2018 Jun 2;430(17):2857–2872. doi: 10.1016/j.jmb.2018.05.042

Table 1:

Thermodynamic parameters for binding of ubiquitin to REV1 UBM1-UBM2 and REV1 UBM2 obtained by ITC

ΔGb ΔHb −TΔSb
Sample Site (N)a KD (μM)b kcal/mol
REV1 UBM1-UBM2 (C958S C977A) 0.8 ± 0.1 18.7 ± 1.6 −6.45 ± 0.05 −1.10 ± 0.13 −5.34 ± 0.18
REV1 UBM2 0.9 ± 0.1 14.9 ± 3.0 −6.59 ± 0.12 −1.17 ± 0.64 −5.41 ± 0.52
a

Binding stoichiometry

b

KD is the dissociation constant. ΔG, ΔH and ΔS are the respective changes in Gibbs free energy, enthalpy, and entropy upon binding at T=298 K.