作者: Ching-Yung Ma , Manoj Kumar Rout , Wing-Man Chan , David Lee Phillips
DOI: 10.1021/JF991222N
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摘要: Analysis of Raman spectra oat globulin showed that extreme pH values caused an increase in the amide and C−H stretching band intensity, indicating changes secondary structures protein due to denaturation. Similar were observed when was treated with chaotropic salts several perturbants. Sodium dodecyl sulfate, β-mercaptoethanol, ethylene glycol also a shift III‘ band, suggesting transition from β-sheet random coil conformation. Heating at temperatures near denaturation temperature led increases unfolding protein. The data indicate FT-Raman spectroscopy is suitable for studying structure plant proteins such as globulin. Keywords: spectroscopy; globulin; conformation