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. 2018 Dec 19;294(8):2892–2902. doi: 10.1074/jbc.RA118.006764

Table 2.

Thermodynamics of Tat-SF1 binding SF3b1 ULMs

Average values and standard deviations of three independent titrations.

Interaction KD ΔH TΔSa
μm kcal mol1
Wildtype Tat-SF1titrated with ULM regions
    SF3b1ULM 1.8 ± 0.9 −66.1 ± 3.0 58.0 ± 3.0
    ULM1 3.0 ± 0.5 −11.8 ± 0.3 4.1 ± 0.3
    ULM2b No detectable binding
    ULM3b No detectable binding
    ULM4c 18.9 ± 4.7 −34.1 ± 25.3 27.5 ± 25.5
    ULM5 0.8 ± 0.1 −18.7 ± 1.0 10.2 ± 1.2
E286K/D290K mutant Tat-SF1 titrated with ULM5
    ULM5b No detectable binding
E286K/F337A mutant Tat-SF1 titrated with ULM5
    ULM5b No detectable binding

a Calculated using −TΔS = ΔGH, with ΔG = −RT ln (KD−1) and T = 303 K.

b No heats detected during titration of 200 μm ULM into 20 μm Tat-SF1 protein.

c Values are estimates due to low binding affinity.