Fourier-transform infrared spectroscopic investigation of the thermal denaturation of hen egg-white lysozyme dissolved in aqueous buffer and glycerol

被引:0
|
作者
Caroline Pérez
Kai Griebenow
机构
[1] University of Puerto Rico,Department of Chemistry, Río Piedras Campus
来源
Biotechnology Letters | 2000年 / 22卷
关键词
folding intermediate; molten globule state; non-aqueous solvent; protein folding; protein stability;
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学科分类号
摘要
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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页码:1899 / 1905
页数:6
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