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傅里叶红外光谱研究血清白蛋白构象
引用本文:童义平,李伟,林燕文.傅里叶红外光谱研究血清白蛋白构象[J].光谱学与光谱分析,1999,19(5):704-706.
作者姓名:童义平  李伟  林燕文
作者单位:韩山师范学院化生系,521041,潮州
摘    要:用傅里叶红外光谱法研究了BSA及其水溶液的红外光谱。通过对其酰胺I带傅里叶自转积谱分析,为其及部分水溶液中的二级结构构象进行了指认。结果表明,BSA水溶液状态与固态时的二级结构是不同的。随着溶液浓度的降低,酰胺I带二级结构峰存在明显的位移现象,即1609.86cm^-1位移到1608.24cm^-1,1633.85位移到1638.36cm^-1,1653.69cm^-1位移到1656.10cm^-

关 键 词:傅里叶红外光谱  牛血清白蛋白  二级结构  构象  自转积

Study of Conformation of Serum Albumin by FTIR
Yiping TONG,Wei LI,Yanwen LIN.Study of Conformation of Serum Albumin by FTIR[J].Spectroscopy and Spectral Analysis,1999,19(5):704-706.
Authors:Yiping TONG  Wei LI  Yanwen LIN
Institution:Department of Bio-Chemistry, Hanshan Teacher's College, 521041 Chaozhou.
Abstract:This paper used the FTIR method to study the spectra of bovine serum albumin (BSA) and its solution. The secondary structure and conformation was assigned by FTIR-deconvolution analysis. The result indicated that BSA secondary structure in solid is different from in aqueous solution. As the decrease of BSA concentration from 3.241 x 10(-1) to 4.032 X 10(-2) g X mL(-1), the amide I band components at 1 609.84, 1 633.85,1 653.69, 1 681.16 and 1 694.88 cm(-1) shifted to 1 608. 24, 1 638.36, 1 656.10, 1 674.87 and 1 690.78 cm(-1), respectively, the component at 1 621.50 cm(-1) unchanged.
Keywords:FTIR    Bovine serum albumin    Secondary structure    Conformation    Deconvolution
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