Folding of the protein domain hbSBD

Maksim Kouza, Chi Fon Chang, Shura Hayryan, Tsan Hung Yu, Mai Suan Li, Tai Huang Huang*, Chin Kun Hu

*此作品的通信作者

研究成果: 雜誌貢獻期刊論文同行評審

30 引文 斯高帕斯(Scopus)

摘要

The folding of the α-helix domain hbSBD of the mammalian mitochondrial branched-chain α-ketoacid dehydrogenase complex is studied by the circular dichroism technique in absence of urea. Thermal denaturation is used to evaluate various thermodynamic parameters defining the equilibrium unfolding, which is well described by the two-state model with the folding temperature TF = 317.8 ± 1.95 K and the enthalpy change ΔHG = 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 α-ketoacid dehydrogenase.

原文英語
頁(從 - 到)3353-3361
頁數9
期刊Biophysical Journal
89
發行號5
DOIs
出版狀態已發佈 - 2005 十一月

ASJC Scopus subject areas

  • 生物物理學

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