Raman spectroscopic study of oat globulin conformation

被引:39
作者
Ma, CY [1 ]
Rout, MK
Chan, WM
Phillips, DL
机构
[1] Univ Hong Kong, Dept Bot, Food Sci Lab, Hong Kong, Hong Kong, Peoples R China
[2] Univ Hong Kong, Dept Chem, Hong Kong, Hong Kong, Peoples R China
关键词
Raman spectroscopy; oat globulin; protein conformation;
D O I
10.1021/jf991222n
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
Analysis of Raman spectra of oat globulin showed that extreme pH values caused an increase in the amide and C-H stretching band intensity, indicating changes in the secondary structures of the protein due to denaturation. Similar changes were observed when oat globulin was treated with chaotropic salts and several protein perturbants. Sodium dodecyl sulfate, beta-mercaptoethanol, and ethylene glycol also caused a shift in the amide III' band, suggesting a transition from beta-sheet to a random coil conformation. Heating at temperatures near the denaturation temperature of oat globulin led to increases in the amide and C-H band intensity, indicating unfolding of the protein. The data indicate that FT-Raman spectroscopy is suitable for studying the secondary structure of plant proteins such as oat globulin.
引用
收藏
页码:1542 / 1547
页数:6
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