The lysine and methionine rich basic subunit of buckwheat grain legumin: some results of a structural study.
The 26 kD basic subunit of 280 kD buckwheat grain legumin has been partially characterized by measurement of its fluorescence and CD spectra. The protein has 22% alpha-helix, 36% beta-sheet, 12% beta-turn and 30% random coil secondary structure. In comparison with the basic subunits of other legumin-type proteins, the buckwheat legumin subunit has a high content of lysine and methionine. The protein also has higher ratios of lysine to arginine and methionine to arginine.
Department of Botany, North Eastern Hill University, Shillong, India.
M K
MK
Rout
N K
NK
Chrungoo
D001120:Arginine / Q000032:analysis; D002942:Circular Dichroism; D019612:Fagopyrum; D008239:Lysine / Q000032:analysis*; D008715:Methionine / Q000032:analysis*; D010940:Plant Proteins / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence; D000097793:Legumins
D001120:Arginine; D008239:Lysine; D008715:Methionine; D010940:Plant Proteins; D000097793:Legumins