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

doi:10.1529/biophysj.105.065151

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

^*Corresponding author for this work

Department of Physics

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

30 Citations (Scopus)

Abstract

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 T_F = 317.8 ± 1.95 K and the enthalpy change ΔH_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 α-ketoacid dehydrogenase.

Original language	English
Pages (from-to)	3353-3361
Number of pages	9
Journal	Biophysical Journal
Volume	89
Issue number	5
DOIs	https://doi.org/10.1529/biophysj.105.065151
Publication status	Published - 2005 Nov

ASJC Scopus subject areas

Biophysics

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10.1529/biophysj.105.065151

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title = "Folding of the protein domain hbSBD",

abstract = "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.",

author = "Maksim Kouza and Chang, {Chi Fon} and Shura Hayryan and Yu, {Tsan Hung} and Li, {Mai Suan} and Huang, {Tai Huang} and Hu, {Chin Kun}",

note = "Funding Information: This work was supported by KBN-State Committee for Scientific Research (grant No. 1P03B01827), National Science Council in Taiwan (grant Nos. NSC 93-2112-M-001-027 and 94-2119-M-002-001 to C.K.H. and grant No. NSC 92-2113-M-001-056 to T.H.H.), and by Academia Sinica in Taiwan (grant No. AS-92-TP-A09). ",

year = "2005",

month = nov,

doi = "10.1529/biophysj.105.065151",

language = "English",

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AU - Kouza, Maksim

AU - Chang, Chi Fon

AU - Hayryan, Shura

AU - Yu, Tsan Hung

AU - Li, Mai Suan

AU - Huang, Tai Huang

AU - Hu, Chin Kun

N1 - Funding Information: This work was supported by KBN-State Committee for Scientific Research (grant No. 1P03B01827), National Science Council in Taiwan (grant Nos. NSC 93-2112-M-001-027 and 94-2119-M-002-001 to C.K.H. and grant No. NSC 92-2113-M-001-056 to T.H.H.), and by Academia Sinica in Taiwan (grant No. AS-92-TP-A09).

PY - 2005/11

Y1 - 2005/11

N2 - 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.

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Folding of the protein domain hbSBD

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