Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II

Tan Cui-Yan; Xu Chun-He; Shen Jun-Ren; Sakuma Shinsuke; Yamamoto Yasushi; Balny Claude; Ruan Kang-Cheng

Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II

Tan Cui-Yan, Xu Chun-He, Shen Jun-Ren, Sakuma Shinsuke, Yamamoto Yasushi, Balny Claude, Ruan Kang-Cheng

Research output: Contribution to journal › Article › peer-review

Abstract

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°C and 3°C, respectively. The standard free energy and standard volume change of the protein for unfolding at 20°C is 23.45 kJ/mol and -150.3 ml/mol, respectively. Kinetics study indicated that at 20°C the activation volume for unfolding, Δ V_u ^‡, was negative (-66.2 ml/mol), meanwhile the activation volume for folding, Δ V_f^‡, was positive (84. 1 ml/mol). The rate constants for folding and unfolding (K_0f, K _0u) were 1.87 s^-1 and 1.3 × 10^-4 s ^-1, respectively, these results provide some clues to explain why the protein is so sensitive to pressure.

Original language	English
Pages (from-to)	677-681
Number of pages	5
Journal	Acta Biochimica et Biophysica Sinica
Volume	35
Issue number	7
Publication status	Published - Aug 22 2003
Externally published	Yes

Keywords

Fluorescence spectroscopy
High pressure technique
Protein unfolding

ASJC Scopus subject areas

Biophysics
Biochemistry

Cite this

@article{765193fdeaf1402c80469f0746022b8d,

title = "Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II",

abstract = "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°C and 3°C, respectively. The standard free energy and standard volume change of the protein for unfolding at 20°C is 23.45 kJ/mol and -150.3 ml/mol, respectively. Kinetics study indicated that at 20°C the activation volume for unfolding, Δ Vu ‡, was negative (-66.2 ml/mol), meanwhile the activation volume for folding, Δ Vf‡, was positive (84. 1 ml/mol). The rate constants for folding and unfolding (K0f, K 0u) were 1.87 s-1 and 1.3 × 10-4 s -1, respectively, these results provide some clues to explain why the protein is so sensitive to pressure.",

keywords = "Fluorescence spectroscopy, High pressure technique, Protein unfolding",

author = "Tan Cui-Yan and Xu Chun-He and Shen Jun-Ren and Sakuma Shinsuke and Yamamoto Yasushi and Balny Claude and Ruan Kang-Cheng",

year = "2003",

month = aug,

day = "22",

language = "English",

volume = "35",

pages = "677--681",

journal = "Acta Biochimica et Biophysica Sinica",

issn = "1672-9145",

publisher = "Oxford University Press",

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TY - JOUR

T1 - Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II

AU - Cui-Yan, Tan

AU - Chun-He, Xu

AU - Jun-Ren, Shen

AU - Shinsuke, Sakuma

AU - Yasushi, Yamamoto

AU - Claude, Balny

AU - Kang-Cheng, Ruan

PY - 2003/8/22

Y1 - 2003/8/22

N2 - 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°C and 3°C, respectively. The standard free energy and standard volume change of the protein for unfolding at 20°C is 23.45 kJ/mol and -150.3 ml/mol, respectively. Kinetics study indicated that at 20°C the activation volume for unfolding, Δ Vu ‡, was negative (-66.2 ml/mol), meanwhile the activation volume for folding, Δ Vf‡, was positive (84. 1 ml/mol). The rate constants for folding and unfolding (K0f, K 0u) were 1.87 s-1 and 1.3 × 10-4 s -1, respectively, these results provide some clues to explain why the protein is so sensitive to pressure.

AB - 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°C and 3°C, respectively. The standard free energy and standard volume change of the protein for unfolding at 20°C is 23.45 kJ/mol and -150.3 ml/mol, respectively. Kinetics study indicated that at 20°C the activation volume for unfolding, Δ Vu ‡, was negative (-66.2 ml/mol), meanwhile the activation volume for folding, Δ Vf‡, was positive (84. 1 ml/mol). The rate constants for folding and unfolding (K0f, K 0u) were 1.87 s-1 and 1.3 × 10-4 s -1, respectively, these results provide some clues to explain why the protein is so sensitive to pressure.

KW - Fluorescence spectroscopy

KW - High pressure technique

KW - Protein unfolding

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M3 - Article

C2 - 12883641

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VL - 35

SP - 677

EP - 681

JO - Acta Biochimica et Biophysica Sinica

JF - Acta Biochimica et Biophysica Sinica

SN - 1672-9145

IS - 7

ER -

Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II

Abstract

Keywords

ASJC Scopus subject areas

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