Specificity of amide VI band (FTIR) in globular protein stability

被引：0

作者：

Velusamy, V. ^{[1
]}

Palaniappan, L. ^{[2
]}

Rajagopalan, V. ^{[3
]}

机构：

[1] Kongu Engn Coll, Dept Phys, Perundurai 638052, Tamil Nadu, India

[2] Annamalai Univ, Dept Phys DDE, Annamalainagar 608002, Tamil Nadu, India

[3] Paavai Coll Engn, Dept Phys, Namakkal 637018, Tamil Nadu, India

来源：

JOURNAL OF THE INDIAN CHEMICAL SOCIETY | 2015年 / 92卷 / 04期

关键词：

Globular protein; denaturation; secondary structure; amide VI band; CRYSTAL-STRUCTURE; OVALBUMIN; SERPINS; IMPACT; FORM;

D O I：

暂无

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Generally stabilization of globular proteins are attained by adding cosolvent glucose to resist denaturation due to extremes of pH in both acidic and alkaline region. In this work, the Fourier Transform Infrared (FTIR) spectra were recorded for ovalbumin protein with and without cosolvent (glucose) at pH 2, 5, 7, 9 and 12 in phosphate buffer. The changes hi the secondary structures (alpha-helix, beta-sheets and others) of ovalbumin caused by pH and influence of glucose on them were studied by FTIR spectra. These spectral examinations are specifically made in the amide VI band region towards the secondary structure of proteins since it was not analyzed yet. This analysis verify the stability of protein have good agreement with studies reported previously.

引用

页码：577 / 580

页数：4

共 18 条

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