Folding of the protein domain hbSBD

被引：31

作者：

Kouza, M

Chang, CF

Hayryan, S

Yu, TH

Li, MS

Huang, TH ^{[1
]}

Hu, CK

机构：

[1] Acad Sinica, Inst Biomed Sci, Taipei 11529, Taiwan

[2] Acad Sinica, Gen Res Ctr, Taipei 11529, Taiwan

[3] Acad Sinica, Inst Phys, Taipei 11529, Taiwan

[4] Polish Acad Sci, Inst Phys, PL-02668 Warsaw, Poland

[5] Natl Taiwan Normal Univ, Dept Phys, Taipei 11718, Taiwan

[6] Natl Taiwan Univ, Div Phys, Natl Ctr Theoret Sci Taipei, Taipei 10617, Taiwan

来源：

BIOPHYSICAL JOURNAL | 2005年 / 89卷 / 05期

关键词：

D O I：

10.1529/biophysj.105.065151

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The folding of the alpha-helix domain hbSBD of the mammalian mitochondrial branched-chain alpha-ketoacid dehydrogenase complex is studied by the circular dichroism technique in absence of urea. Thermal denaturation is used to evaluate various thermodynamic parameters de. ning the equilibrium unfolding, which is well described by the two-state model with the folding temperature T-F 317.8 +/- 1.95 K and the enthalpy change Delta H-G 19.67 +/- 2.67 kcal/mol. The folding is also studied numerically using the off-lattice coarse-grained Go model and the Langevin dynamics. The obtained results, including the population of the native basin, the free-energy landscape as a function of the number of native contacts, and the folding kinetics, also suggest that the hbSBD domain is a two-state folder. These results are consistent with the biological function of hbSBD in branched-chain alpha-ketoacid dehydrogenase.

引用

页码：3353 / 3361

页数：9

共 42 条

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