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. 2011 Sep 14;286(44):38478–38487. doi: 10.1074/jbc.M111.265710

TABLE 2.

Thermodynamic constants determined by ITC

S.D. results from at least two experiments. The peptides used in this experiment are listed under supplemental Table S1.

N KD ΔH TΔS
μm kJ/mol
Smb-1
    WT 2.1 ± 0.1 295 ± 70 −21 ± 1 2 ± 1

Smb-2
    WT 1.04 ± 0.02 20 ± 1 −37 ± 2 10 ± 2
    W29A 1.15 ± 0.20 62 ± 10 −38 ± 3 16 ± 3
    W70A 0.98 ± 0.06 60 ± 1 −35 ± 1 12 ± 1
    Δ35–41 1.05 ± 0.02 26 ± 4 −37 ± 2 13 ± 2
    Δ33–44 0.98 ± 0.02 33 ± 12 −21 ± 5 −3 ± 6
    Glycine linker 0.99 ± 0.09 40 ± 9 −46 ± 5 23 ± 6

Smb-4
    WT 1.03 ± 0.02 4.5 ± 0.2 −65 ± 4 37 ± 5
    W29A 0.74 ± 0.02 50 ± 5 −51 ± 1 28 ± 1
    W70A 0.72 ± 0.03 35 ± 2 −55 ± 4 31 ± 4
    Δ35–41 1.02 ± 0.01 2.7 ± 0.1 −61 ± 1 32 ± 1
    Δ33–44 1.04 ± 0.02 1.8 ± 0. 3 −53 ± 2 22 ± 2
    Glycine linker 1.05 ± 0.02 4.7 ± 0. 2 −62 ± 1 33 ± 1

SF3B4–1
    WT 2.0 ± 0.1 570 ± 5 −8 ± 1 −9 ± 1

SF3B4–2
    WT 1.02 ± 0.02 38 ± 2 −30 ± 1 6 ± 1
    W29A 1.04 ± 0.03 134 ± 32 −27 ± 1 7 ± 1
    W70A 1.12 ± 0.10 91 ± 11 −19 ± 1 −3 ± 1
    Δ35–41 1.03 ± 0.01 38 ± 4 −34 ± 2 10 ± 2
    Δ33–44 NDa ND ND ND
    Glycine linker 1.11 ± 0.07 43 ± 5 −35 ± 8 12 ± 8

a ND, not determined.