Effects of solute-matrix interaction on monitoring the conformational changes of immobilized proteins by surface plasmon resonance sensor.
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.
Chen
Liang-Yu
LY
Department of Chemical and Materials Engineering, National Central University, Chung-Li, Taiwan.
Wu
Ming-Chia
MC
Chou
Mao-Tsun
MT
Kao
Li-An
LA
Chen
Shean-Jen
SJ
Chen
Wen-Yih
WY