《Table 1 Tentative assignment of glycinin in Raman spectra》

  提示：宽带有限、当前游客访问压缩模式

本系列图表出处文件名：随高清版一同展现

《Study on Isolation and Raman Spectroscopy of Glycinin in Soybean Protein》

1. 获取 高清版本忘记账户？点击这里登录

1. 下载图表忘记账户？点击这里登录

The doublet at 850 and 830 cm-1in the Raman spectra of proteins containing tyrosyl residues was examined to determine its origin and detect Fermi resonance between the symmetric ring-breathing vibration and overtone of the out-of-plane vibration of the para-substituted benzene ring.This information could also reflect whether the tyrosine residues of proteins were exposed or buried[7].When I850/I830 was 1.25–1.40，0.7，and 0.3–0.5，the residues representing tyrosine were completely exposed，ionized，and embedded in the surface of proteins molecules，respectively[20].In this study，the characteristic band of tyrosine side chains in glycinin was I850/I830=1.145 at 642，834，855，and 1 204 cm-1.Furthermore，in accordance with the N（buried or exposed）calculation method described by Kalapathy[20]，the N-buried and N-exposed tyrosine residues account for 14.1%and 85.9%of the total amount of residues in glycinin，respectively（Table 3）.Thus，the tyrosine residues evaluated in this study tended to be exposed.