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 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 - 2003 |
| Externally published | Yes |
Fingerprint
Keywords
- Fluorescence spectroscopy
- High pressure technique
- Protein unfolding
ASJC Scopus subject areas
- Biochemistry
- Biophysics
Cite this
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 journal › Article
}
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 - Shen, Jian-Ren
AU - Shinsuke, Sakuma
AU - Yasushi, Yamamoto
AU - Claude, Balny
AU - Kang-Cheng, Ruan
PY - 2003
Y1 - 2003
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
UR - http://www.scopus.com/inward/record.url?scp=0042071196&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0042071196&partnerID=8YFLogxK
M3 - Article
C2 - 12883641
AN - SCOPUS:0042071196
VL - 35
SP - 677
EP - 681
JO - Acta Biochimica et Biophysica Sinica
JF - Acta Biochimica et Biophysica Sinica
SN - 1672-9145
IS - 7
ER -