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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

7 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 languageEnglish
Pages (from-to)862-867
Number of pages6
JournalTalanta
Volume67
Issue number4
DOIs
StatePublished - 15 Oct 2005

Keywords

  • Denaturant
  • Protein conformation
  • Refractive index
  • Surface plasmon resonance

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