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. 2003 Oct;12(10):2367–2373. doi: 10.1110/ps.03176803

Table 3.

Thermal denaturation parameters of RNase Sa and six mutants

RNase Td (°C) ΔTda (°C) ΔΔGb (kcal/mole) ΔHcal (kcal/mole) ΔHeff (kcal/mole) Rc
pH 7.0
    Wild type 49.0 92 103 0.89
    Gln38Ala 52.5 3.5 1.0 109 110 0.99
    Glu41Lys 46.5 −2.5 −0.7 90 100 0.90
    Glu54Gln 43.1 −5.9 −1.7 81 87 0.93
    Arg65Ala 45.6 −3.4 −1.0 81 90 0.90
    Glu74Lys 52.1 3.1 0.9 101 113 0.89
    His85Gln 49.1 0.1 0 90 89 1.01
pH 5.5
    Wild type 55.6 97 101 0.96
    Gln38Ala 56.9 1.3 0.4 98 103 0.95
    Glu41Lys 50.5 −5.1 −1.5 97 101 0.96
    Glu54Gln 47.7 −7.9 −2.3 89 92 0.97
    Arg65Ala 51.1 −4.5 −1.3 81 78 1.04
    Glu74Lys 56.0 0.4 0.1 103 99 1.04
    His85Gln 55.5 −0.1 0 94 105 0.90

a ΔTd = Td (mutant) − Td (wild type).

b ΔΔG (= ΔTd × ΔSd) is the difference in the free energies of unfolding of wild-type and mutant RNase Sa at Td, and ΔSd (= ΔHcal/Td) is the entropy of unfolding of wild-type RNase Sa. A negative sign indicates a decrease in stability.

cR = ΔHcalHeff.