dorsal/arxiv
View SchemaFolding of the Protein Domain hbSBD
| Authors | Maksim Kouza, Chi-Fon Chang, Shura Hayryan, Tsan-hung Yu, Mai Suan Li, Tai-huang Huang, Chin-Kun Hu |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0612031 |
| URL | https://arxiv.org/abs/q-bio/0612031 |
| DOI | 10.1529/biophysj.105.065151 |
| Journal | Biophysical J. 89, 3353 (2005) |
Abstract
The folding of the alpha-helice domain hbSBD of the mammalian mitochondrial branched-chain alpha-ketoacid dehydrogenase (BCKD) 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 K and the enthalpy change Delta H_g = 19.67 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 BCKD.
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"abstract": "The folding of the alpha-helice domain hbSBD of the mammalian mitochondrial\nbranched-chain alpha-ketoacid dehydrogenase (BCKD) complex is studied by the\ncircular dichroism technique in absence of urea. Thermal denaturation is used\nto evaluate various thermodynamic parameters defining the equilibrium\nunfolding, which is well described by the two-state model with the folding\ntemperature T_f = 317.8 K and the enthalpy change Delta H_g = 19.67 kcal/mol.\nThe folding is also studied numerically using the off-lattice coarse-grained Go\nmodel and the Langevin dynamics. The obtained results, including the population\nof the native basin, the free energy landscape as a function of the number of\nnative contacts and the folding kinetics, also suggest that the hbSBD domain is\na two-state folder. These results are consistent with the biological function\nof hbSBD in BCKD.",
"arxiv_id": "q-bio/0612031",
"authors": [
"Maksim Kouza",
"Chi-Fon Chang",
"Shura Hayryan",
"Tsan-hung Yu",
"Mai Suan Li",
"Tai-huang Huang",
"Chin-Kun Hu"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1529/biophysj.105.065151",
"journal_ref": "Biophysical J. 89, 3353 (2005)",
"title": "Folding of the Protein Domain hbSBD",
"url": "https://arxiv.org/abs/q-bio/0612031"
},
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