CONFORMATION CHANGES OF BETA-LACTOGLOBULIN - AN ATR INFRARED SPECTROSCOPIC STUDY OF THE EFFECT OF PH AND ETHANOL

被引：31

作者：

DUFOUR, E ^{[1
]}

ROBERT, P ^{[1
]}

BERTRAND, D ^{[1
]}

HAERTLE, T ^{[1
]}

机构：

[1] INRA,LTAN,F-44026 NANTES 03,FRANCE

来源：

JOURNAL OF PROTEIN CHEMISTRY | 1994年 / 13卷 / 02期

关键词：

BETA-LACTOGLOBULIN; STRUCTURE; SOL-GEL TRANSITION; INFRARED; PRINCIPAL COMPONENT ANALYSIS;

D O I：

10.1007/BF01891973

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Fourier transform infrared spectroscopy has been applied to investigate the secondary structural changes of beta-lactoglobulin in water/ethanol mixtures. The studies were carried out at two different pHs and at high protein concentrations. The spectra were recorded using an attenuated total reflection cell. The amide I band of beta-lactoglobulin in water reveals large amounts of intra extended beta-sheet structure. About 20% ethanol, beta-lactoglobulin unfolds and beta-strand formation is observed. alpha-Helices are built up by increasing the ethanol concentration up to 30%. In 50% ethanol, beta-lactoglobulin gels providing the apparent pH are neutral. The secondary structural changes of beta-lactoglobulin were observed on the similarity maps obtained by Principal Component Analysis.

引用

页码：143 / 149

页数：7

共 30 条

[1] STRUCTURAL AND CONFORMATIONAL-CHANGES OF BETA-LACTOGLOBULIN-B - AN INFRARED SPECTROSCOPIC STUDY OF THE EFFECT OF PH AND TEMPERATURE [J].