LYOPHILIZATION-INDUCED REVERSIBLE CHANGES IN THE SECONDARY STRUCTURE OF PROTEINS

被引：333

作者：

GRIEBENOW, K ^{[1
]}

KLIBANOV, AM ^{[1
]}

机构：

[1] MIT, DEPT CHEM, CAMBRIDGE, MA 02139 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1995年 / 92卷 / 24期

关键词：

FOURIER-TRANSFORM INFRARED SPECTROSCOPY; DEHYDRATION; ALPHA-HELIX; BETA-SHEET; SOLID STATE;

D O I：

10.1073/pnas.92.24.10969

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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.

引用

页码：10969 / 10976

页数：8