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

Liang Yu Chen; Ming Chia Wu; Mao Tsun Chou; Li An Kao; Shean Jen Chen; Wen Yih Chen

doi:10.1016/j.talanta.2005.04.047

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

Liang Yu Chen, Ming Chia Wu, Mao Tsun Chou, Li An Kao, Shean Jen Chen, Wen Yih Chen

Department of Chemical and Materials Engineering

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	862-867
Number of pages	6
Journal	Talanta
Volume	67
Issue number	4
DOIs	https://doi.org/10.1016/j.talanta.2005.04.047
State	Published - 15 Oct 2005

Keywords

Denaturant
Protein conformation
Refractive index
Surface plasmon resonance

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10.1016/j.talanta.2005.04.047

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

abstract = "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.",

keywords = "Denaturant, Protein conformation, Refractive index, Surface plasmon resonance",

author = "Chen, {Liang Yu} and Wu, {Ming Chia} and Chou, {Mao Tsun} and Kao, {Li An} and Chen, {Shean Jen} and Chen, {Wen Yih}",

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T1 - Effects of solute-matrix interaction on monitoring the conformational changes of immobilized proteins by surface plasmon resonance sensor

AU - Chen, Liang Yu

AU - Wu, Ming Chia

AU - Chou, Mao Tsun

AU - Kao, Li An

AU - Chen, Shean Jen

AU - Chen, Wen Yih

PY - 2005/10/15

Y1 - 2005/10/15

N2 - 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.

AB - 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.

KW - Denaturant

KW - Protein conformation

KW - Refractive index

KW - Surface plasmon resonance

UR - http://www.scopus.com/inward/record.url?scp=24344454736&partnerID=8YFLogxK

U2 - 10.1016/j.talanta.2005.04.047

DO - 10.1016/j.talanta.2005.04.047

M3 - 期刊論文

C2 - 18970251

AN - SCOPUS:24344454736

SN - 0039-9140

VL - 67

SP - 862

EP - 867

JO - Talanta

JF - Talanta

IS - 4

ER -

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

Abstract

Keywords

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