Abstract

The thermal denaturation of lysozyme dissolved in aqueous phosphate buffer (pH 5.1) and glycerol was studied by Fourier-transform infrared (FTIR) spectroscopy. In both solvents, a single temperature-induced conformational transition was observed but at the distinctly different temperatures of 73 °C in aqueous buffer and 94 ± 2 °C in glycerol. No changes in the secondary structure were observed in glycerol up to 90 °C. Thus, FTIR data were consistent with the formation of a highly ordered molten globule state at temperatures below 90 °C followed by lysozyme unfolding at higher temperatures in glycerol.

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