高等学校化学学报 ›› 2003, Vol. 24 ›› Issue (2): 226-231.

• 论文 • 上一篇    下一篇

红外光谱酰胺Ⅲ带用于蛋白质二级结构的测定研究

谢孟峡, 刘媛   

  1. 北京师范大学分析测试中心, 北京 100875
  • 收稿日期:2002-02-05 出版日期:2003-02-24 发布日期:2003-02-24
  • 通讯作者: 谢孟峡(1962年出生),男,硕士,副教授,主要从事色谱及有机波谱研究.E-mail:mengxia-xie@263.net E-mail:mengxia-xie@263.net
  • 基金资助:

    国家自然科学基金(批准号:39825112)资助

Studies on Amide Ⅲ Infrared Bands for the Secondary Structure Determination of Proteins

XIE Meng-Xia, LIU Yuan   

  1. Analytical & Testing Center, Beijing Normal University, Beijing 100875, China
  • Received:2002-02-05 Online:2003-02-24 Published:2003-02-24

摘要: 用甲醇对BSA和RaseA等蛋白质进行变性处理,结合蛋白质酰胺带的拟合结果对酰胺带各二级结构的谱峰进行了初步指认:1330~1290cm-1为α-螺旋;1295~1265cm-1为β-转角;1270~1245cm-1为无规卷曲;1250~1220cm-1为β-折叠.依据这些谱峰归属,对一些已知二级结构的蛋白质进行了测定,所得结果与X射线衍射数据以及酰胺带的定量结果基本一致.

关键词: 傅里叶变换红外光谱(FTIR), 酰胺Ⅲ带, 蛋白质二级结构, 溶剂变性

Abstract: Fourier transform infrared spectroscopy is increasingly becoming an important method for quantitatively determining the secondary structure of proteins. Amide Ⅰ band(1 600-1 700cm-1) and amide Ⅲ (1 220-1 330cm-1) are two main bands for this purposes. Amide Ⅲ was neglected because of its relatively weak in signals, but there is not interference from water and water vapor vibration bands and it is more sensitive to the changes of protein secondary structure. In this paper, proteins BSA and RNase A were denatured by methanol. The component bands of secondary structure in amide Ⅲ were assigned by combining the quantitative results of amide Ⅰ band. α-Helix 1 330-1 290cm-1; β-turn 1 295-1 265cm-1; Random coil 1 270-1 245cm-1 and β-sheet 1 250-1 220cm-1. The overlapping area between the neighboring bands of different structures, such as 1 290-1 295cm-1, 1 265-1 270cm-1, 1 245-1 250cm-1, can be determined according to quantitative results of amide Ⅰ band. By using above assignments, the quantitative analysis results of the proteins in which the secondary structures have been known were consistent with that of X-ray data and amide Ⅰ band.

Key words: FTIR, Amide Ⅲ band, Secondary structure of proteins, Solvent denaturation

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