Effects of solute-matrix interaction on monitoring the conformational changes of immobilized proteins by surface plasmon resonance sensor

被引：9

作者：

Chen, LY

Wu, MC

Chou, MT

Kao, LA

Chen, SJ

Chen, WY ^{[1
]}

机构：

[1] Natl Cent Univ, Dept Chem & Mat Engn, Chungli 320, Taiwan

[2] Natl Cheng Kung Univ, Dept Engn Sci, Tainan 701, Taiwan

来源：

TALANTA | 2005年 / 67卷 / 04期

关键词：

protein conformation; surface plasmon resonance; refractive index; denaturant;

D O I：

10.1016/j.talanta.2005.04.047

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

A real-time and labeling-free surface plasmon resonance (SPR) sensor was used to monitor the conformational changes of immobilized globule proteins (RNase A and lysozyme) in chemical unfolding and refolding. The effects of chemical denaturants on the protein structures were investigated. The methodology in protein conformational study on the solid surface is refined through the theoretic calculations and the conformational information of native/denatured proteins in solution. Additionally, our observation illustrates that the ambient buffer solution is merit to influence the refractive index of immobilized protein films and directly be observed from the SPR resonance angle shifts. (c) 2005 Elsevier B.V. All rights reserved.

引用

页码：862 / 867

页数：6

共 42 条

[1] Conformational changes of β-lactoglobulin in sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles -: A fluorescence and CD study [J].