| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10561420 | Talanta | 2005 | 6 Pages |
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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Liang-Yu Chen, Ming-Chia Wu, Mao-Tsun Chou, Li-An Kao, Shean-Jen Chen, Wen-Yih Chen,