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

被引:24
|
作者
Pérez, C [1 ]
Griebenow, K [1 ]
机构
[1] Univ Puerto Rico, Dept Chem, San Juan, PR 00931 USA
基金
美国国家科学基金会; 美国国家卫生研究院;
关键词
folding intermediate; molten globule state; non-aqueous solvent; protein folding; protein stability;
D O I
10.1023/A:1005645810247
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
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 degreesC in aqueous buffer and 94 +/- 2 degreesC in glycerol. No changes in the secondary structure were observed in glycerol up to 90 degreesC. Thus, FTIR data were consistent with the formation of a highly ordered molten globule state at temperatures below 90 degreesC followed by lysozyme unfolding at higher temperatures in glycerol.
引用
收藏
页码:1899 / 1905
页数:7
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