Figure 1From: Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteinsThermodynamic stability profiles of RNases H. Open circles represent the temperature dependence of ΔG(H2O) of Tm-RNase HII at pH 7.5; open triangles, those of Aa-RNase HII at pH 5.0; and closed squares, those of Sto-RNase HI at pH 3.0. The Tm at which ΔG(H2O) becomes zero were estimated from the heat-induced unfolding experiments. The lines represent the fit of Eq. (3). Long-dashed line represents the stability profiles of Tk-RNase HII; the short-dashed line, that of Tt-RNase HI; and the one-point dashed line, that of Ec-RNase HI [19, 20].Back to article page