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The equilibrium unfolding of hen lysozyme at pH 2 was studied as a function of pressure (0.1~700MPa) and temperature (-10°C~50°C) using Trp fluorescence as monitor supplemented by variable pressure 1 H NMR spectroscopy (0.1~400MPa). The unfolding profiles monitored by the two methods allowed the two-state equilibrium analysis between the folded (N) and unfolded (U) conformers. The free energy differences Δ G (= G  U - G  N ) were evaluated from changes in the wavelength of maximum fluorescence intensity ( λ  max ) as a function of pressure and temperature. The dependence of Δ G on temperature exhibits concave curvatures against temperature, showing positive heat capacity changes (Δ C   p  = C   p   U - C   p   N = 1.8-1.9 kJ mol -1 deg -1 ) at all pressures studied (250~400 MPa), while the temperature T  S for maximal Δ G increased from about 10°C at 250MPa to about 40°C at 550MPa. The dependence of Δ G on pressure gave negative volume changes (Δ V = V  U - V  N ) upon unfolding at all temperatures studied (-86~-17 mlmol -1 for -10°C~50°C), which increase significantly with increasing temperature, giving a positive expansivity change (Δ α ~1.07mlmol -1 deg -1 ). A phase-diagram between N and U (for Δ G =0) is drawn of hen lysozyme at pH 2 on the pressure-temperature plane. Finally, a three-dimensional free energy landscape (Δ G ) is presented on the p-T plane.

The pressure-temperature phase diagram of hen lysozyme at low pH