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

ABSTRACT: 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 ¹H 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 ΔG (=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 ΔG on temperature exhibits concave curvatures against temperature, showing positive heat capacity changes (ΔC_p =C_p

SUBMITTER: Maeno A 

PROVIDER: S-EPMC5036640 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature