FTIR study of secondary structure of bovine serum albumin and ovalbumin

被引：84

作者：

Abrosimova, K. V. ^{[1
]}

Shulenina, O. V. ^{[1
]}

Paston, S. V. ^{[1
]}

机构：

[1] St Petersburg State Univ, Dept Mol Biophys & Polymer Phys, Ulyanovskaya St 3, St Petersburg, Russia

来源：

18TH INTERNATIONAL CONFERENCE PHYSICA.SPB | 2016年 / 769卷

关键词：

SPECTROSCOPY; PROTEINS; HEAT;

D O I：

10.1088/1742-6596/769/1/012016

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

Proteins structure is the critical factor for their functioning. Fourier transform infrared spectroscopy provides a possibility to obtain information about secondary structure of proteins in different states and also in a whole biological samples. Infrared spectra of egg white from the untreated and hard-boiled hen's egg, and also of chicken ovalbumin and bovine serum albumin in lyophilic form and in aqueous solution were studied. Lyophilization of investigated globular proteins is accompanied by the decrease of alpha-helix structures and the increase in amount of intermolecular beta-sheets. Analysis of infrared spectrum of egg white allowed to make an estimation of OVA secondary structure and to observe alpha-to-beta structural transformation as a result of the heat denaturation.

引用

页数：6

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