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

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

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)677-681
Number of pages5
JournalActa Biochimica et Biophysica Sinica
Volume35
Issue number7
Publication statusPublished - 2003
Externally publishedYes

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Protein Unfolding
Photosystem II Protein Complex
Spinacia oleracea
Thermodynamics
Kinetics
Pressure
Proteins
Chemical activation
Fluorescence Spectrometry
Fluorescence spectroscopy
Hot Temperature
Free energy
Rate constants

Keywords

  • Fluorescence spectroscopy
  • High pressure technique
  • Protein unfolding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics

Cite this

Cui-Yan, T., Chun-He, X., Shen, J-R., Shinsuke, S., Yasushi, Y., Claude, B., & Kang-Cheng, R. (2003). Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II. Acta Biochimica et Biophysica Sinica, 35(7), 677-681.

Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II. / Cui-Yan, Tan; Chun-He, Xu; Shen, Jian-Ren; Shinsuke, Sakuma; Yasushi, Yamamoto; Claude, Balny; Kang-Cheng, Ruan.

In: Acta Biochimica et Biophysica Sinica, Vol. 35, No. 7, 2003, p. 677-681.

Research output: Contribution to journalArticle

Cui-Yan, T, Chun-He, X, Shen, J-R, Shinsuke, S, Yasushi, Y, Claude, B & Kang-Cheng, R 2003, 'Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II', Acta Biochimica et Biophysica Sinica, vol. 35, no. 7, pp. 677-681.
Cui-Yan, Tan ; Chun-He, Xu ; Shen, Jian-Ren ; Shinsuke, Sakuma ; Yasushi, Yamamoto ; Claude, Balny ; Kang-Cheng, Ruan. / Thermodynamic and kinetic analysis of unfolding of P23k protein isolated from spinach photosystem II. In: Acta Biochimica et Biophysica Sinica. 2003 ; Vol. 35, No. 7. pp. 677-681.
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AU - Yasushi, Yamamoto

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AU - Kang-Cheng, Ruan

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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.

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