title: Folding studies of two hydrostatic pressure sensitive proteins.
abstract: High hydrostatic pressure combined with various spectroscopies is a powerful technique to study protein folding. An ideal model system for protein folding studies should have the following characteristics. (1) The protein should be sensitive to pressure, so that the protein can be unfolded under mild pressure. (2) The folding process of the protein should be easily modulated by several chemical or physical factors. (3) The folding process should be easily monitored by some spectroscopic parameters. Here, we summarized the pressure induced folding studies of two proteins isolated from spinach photosystem II, namely the 23-kDa and the 33-kDa protein. They have all the characteristics mention above and might be an ideal model protein system for pressure studies.
authors.affiliation: Key Laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031, China.
authors.forename: Cui-Yan
authors.initials: CY
authors.lastname: Tan
authors.forename: Chun-He
authors.initials: CH
authors.lastname: Xu
authors.forename: Kang-Cheng
authors.initials: KC
authors.lastname: Ruan
mesh_terms: D006874:Hydrostatic Pressure; D007700:Kinetics; D045332:Photosystem II Protein Complex / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D017510:Protein Folding; D013050:Spectrometry, Fluorescence; D018724:Spinacia oleracea / Q000378:metabolism; D013696:Temperature
chemical_list: D045332:Photosystem II Protein Complex; D010940:Plant Proteins