LYOPHILIZATION-INDUCED REVERSIBLE CHANGES IN THE SECONDARY STRUCTURE OF PROTEINS
LYOPHILIZATION-INDUCED REVERSIBLE CHANGES IN THE SECONDARY STRUCTURE OF PROTEINS
复制标题
DOI：
10.1073/pnas.92.24.10969
复制
发表时间：
1995-11-21
影响因子：
11.1
通讯作者：
KLIBANOV, AM
中科院分区：
文献类型：
--
作者：
GRIEBENOW, K;KLIBANOV, AM
用傅里叶变换红外光谱研究了十几种不同蛋白质水溶液冷冻干燥后二级结构的变化。二阶导数光谱的定量分析和原始红外光谱的高斯曲线拟合都表明，脱水显著(但可逆)改变了所研究的所有蛋白质的二级结构。冷冻干燥大大增加了β-折叠的含量，降低了所有蛋白质的α-螺旋含量。在所有情况下，除了一种情况外，冷冻干燥后蛋白质变得更有序。
Changes in the secondary structure of some dozen different proteins upon lyophilization of their aqueous solutions have been investigated by means of Fourier-transform infrared spectroscopy in the amide III band region. Dehydration markedly (but reversibly) alters the secondary structure of all the proteins studied, as revealed by both the quantitative analysis of the second derivative spectra and the Gaussian curve fitting of the original infrared spectra. Lyophilization substantially increases the beta-sheet content and lowers the alpha-helix content of all proteins. In all but one case, proteins become more ordered upon lyophilization.