冻干诱导的蛋白质二级结构可逆变化。
Lyophilization-induced reversible changes in the secondary structure of proteins.
作者信息
Griebenow K, Klibanov A M
机构信息
Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139, USA.
出版信息
Proc Natl Acad Sci U S A. 1995 Nov 21;92(24):10969-76. doi: 10.1073/pnas.92.24.10969.
Abstract
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.
摘要
通过傅里叶变换红外光谱法在酰胺III带区域研究了大约十二种不同蛋白质的水溶液冻干后二级结构的变化。如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所示，脱水显著（但可逆）改变了所有研究蛋白质的二级结构。冻干显著增加了所有蛋白质的β-折叠含量并降低了α-螺旋含量。除了一种情况外，所有蛋白质在冻干后变得更加有序。
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