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Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Folding studies of two hydrostatic pressure sensitive proteins
Cui-Yan Tan1, Chun-He Xu, Kang-Cheng Ruan
1Key Laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031, China.
Biochimica Et Biophysica Acta
|February 1, 2006
Summary
High hydrostatic pressure is a powerful tool for studying protein folding. Spinach photosystem II proteins (23-kDa and 33-kDa) are ideal model systems due to their pressure sensitivity and easily monitored folding.
Area of Science:
- Biochemistry
- Protein Science
- Spectroscopy
Background:
- High hydrostatic pressure combined with spectroscopy is effective for protein folding studies.
- Ideal model systems for protein folding research are pressure-sensitive, easily modulated, and spectroscopically monitorable.
Purpose of the Study:
- To summarize pressure-induced folding studies of two proteins from spinach photosystem II.
- To evaluate these proteins as potential model systems for pressure-induced folding research.
Main Methods:
- High hydrostatic pressure application.
- Spectroscopic techniques for monitoring protein folding.
- Isolation and characterization of spinach photosystem II proteins (23-kDa and 33-kDa).
Main Results:
- The 23-kDa and 33-kDa spinach photosystem II proteins exhibit pressure-induced folding.
- These proteins demonstrate sensitivity to pressure, allowing unfolding under mild conditions.
- Their folding processes are readily modulated and monitored spectroscopically.
Conclusions:
- The 23-kDa and 33-kDa proteins from spinach photosystem II possess characteristics of ideal model systems for pressure studies.
- These proteins are suitable for investigating pressure-induced folding mechanisms.
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