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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Pérez, C., Griebenow, K. Fourier-transform infrared spectroscopic investigation of the thermal denaturation of hen egg-white lysozyme dissolved in aqueous buffer and glycerol. Biotechnology Letters 22, 1899–1905 (2000). https://doi.org/10.1023/A:1005645810247
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DOI: https://doi.org/10.1023/A:1005645810247