[Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II].
The unfolding of 23kD (P23k) protein isolated from spinach photosystem II particle was studied by high pressure and fluorescence spectroscopy. The thermal equilibrium study indicated that the protein could be totally unfolded by 180 or 160 MPa at 20 degrees C and 3 degrees C, respectively. The standard free energy and standard volume change of the protein for unfolding at 20 degrees C is 23.45 kJ/mol and -150.3 ml/mol, respectively. Kinetics study indicated that at 20 degrees C the activation volume for unfolding, delta V(u)(++), was negative (-66.2 ml/mol), meanwhile the activation volume for folding, deltaV(f)(++), was positive (84.1 ml/mol). The rate constants for folding and unfolding (K(0f), K(0u)) were 1.87 s(-1) and 1.3x10(-4) s(-1), respectively, these results provide some clues to explain why the protein is so sensitive to pressure.
Tan
Cui-Yan
CY
Key Laboratory of Proteomics, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai 200031, China.
Xu
Chun-He
CH
Shen
Jun-Ren
JR
Sakuma
Shinsuke
S
Yamamoto
Yasushi
Y
Balny
Claude
C
Ruan
Kang-Cheng
KC
D007700:Kinetics; D045332:Photosystem II Protein Complex / Q000032:analysis*; D010940:Plant Proteins / Q000737:chemistry*; D011312:Pressure; D017510:Protein Folding; D018724:Spinacia oleracea / Q000737:chemistry*; D013816:Thermodynamics
D045332:Photosystem II Protein Complex; D010940:Plant Proteins