大豆タンパク質の二次構造(II) : グリシニンとβ-コングリシニンのレーザーラマンスペクトルに関する研究

概要

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Laser Raman spectra of soybean glycinin and β-conglycinin in neutral solution are presented. In the native spectra of the both native proteins, the amide III band of glycinin appears a peak at 1,245cm^<-1> and a shoulder peak at 1,235cm^<-1>, and that of β-conglycinin does two peaks at 1,240 and 1,250cm^<-1>. These bands are assigned to the presence of β-sheet structure. From these intensity, using a procedure described by Pezolet et al, we evaluate the β-structure content of glycinin and β-conglycinin to 28% and 24%, respectively. Also, from the backbone amide vibrations at 1,240 cm^<-1> in H_2O (amide III), and 1,632 and 1,660 cm^<-1> in ^2H_2O (amide I'), and methylene band at 1,448cm^<-1> of standards, using the method of Lippert et al the fraction of residues in the helix, β-structure and randam coil conformations is evaluated for glycinin and β-conglycinin.
八戸工業高等専門学校の論文
2004-12-20