16 June 2004 Studying protein structural changes based on surface plasmon resonance and surface-enhanced Raman scattering
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Abstract
The ability to recognize the conformational changes and structural variations of a protein when immobilized in a solid surface is of great importance in a variety of applications. Surface plasmon resonance (SPR) sensing is an appropriate technique for investigating interfacial phenomena, and enables the conformational changes of proteins to be monitored through the variation in the SPR angle shift. Meanwhile, the surface-enhanced Raman scattering (SERS) system can also assist in clarifying the changes in protein structure. The present study utilizes a 1 mM CrO3 phosphate buffer solution (PBS) to induce conformational changes of human serum albumin (HSA). Monitoring the corresponding SPR angle shifts and the SPR reflectivity spectrum enables the relationships between the conformational changes of the surface-immobilized protein and the thickness and dielectric constants of the protein layer to be estimated. The experimental SPR results indicate that the Cr6+ ions cause significant conformational change of the protein. It is established that the ions are not merely absorbed into the protein as a result of electrostatic forces, but that complex protein refolding events also take place. Furthermore, the data acquired from the SERS system yield valuable information regarding the changes which take place in the protein structure.
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Wen-Pin Hu, Wen-Pin Hu, Shean-Jen Chen, Shean-Jen Chen, Jenq-Nan Yih, Jenq-Nan Yih, G.-Y. Lin, G.-Y. Lin, Guan Liang Chang, Guan Liang Chang, } "Studying protein structural changes based on surface plasmon resonance and surface-enhanced Raman scattering", Proc. SPIE 5327, Plasmonics in Biology and Medicine, (16 June 2004); doi: 10.1117/12.530593; https://doi.org/10.1117/12.530593
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