Folding of the protein domain hbSBD.
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 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 DeltaH(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.
Kouza
Maksim
M
Institute of Physics, Polish Academy of Sciences, 02-668 Warsaw, Poland.
Chang
Chi-Fon
CF
Hayryan
Shura
S
Yu
Tsan-hung
TH
Li
Mai Suan
MS
Huang
Tai-huang
TH
Hu
Chin-Kun
CK
D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide) / Q000737:chemistry*; D000818:Animals; D002942:Circular Dichroism; D004926:Escherichia coli / Q000378:metabolism; D006358:Hot Temperature; D007700:Kinetics; D008958:Models, Molecular; D015233:Models, Statistical; D010957:Plasmids / Q000378:metabolism; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D013696:Temperature; D013816:Thermodynamics; D013997:Time Factors
D042942:3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)