Raman spectroscopic study of oat globulin conformation.
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.
Ma
C Y
CY
Food Science Laboratory, Department of Botany, and Department of Chemistry, The University of Hong Kong, Hong Kong. macy@hkucc.hku.hk
Rout
M K
MK
Chan
W M
WM
Phillips
D L
DL
D018554:Avena / Q000737:chemistry*; D005583:Fourier Analysis; D005916:Globulins / Q000737:chemistry*; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman
D005916:Globulins