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
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 Tf = 317.8 K and the enthalpy change Delta Hg = 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.
Create a lesson
Related papers
A meta-algorithm for ab initio reconstruction of complex mixtures in cryo-EM
Alkin Kaz, Arda Kaz, Ellen D. Zhong
PHASE: encoding global protein ensembles with local Hamiltonians and all-atom backmapping
Daniele Angioletti, Marco Nobile, Matteo Carli et al.
Analysis of correlations of dwell-times of adjacent kinetic states in the activity of the cold and menthol receptor TRPM8
Ogloblya O. V., Moroz O. F., Zholos A.
Multitask Bayesian Neural Networks for Multiparameter Protein Engineering
Fabio Herrera-Rocha, David Medina-Ortiz, Desiree Wyrzykala et al.
Recovering protein conformations from single-particle cryo-EM data via indirect shape matching gradient flows
Erik Jansson, Jonathan Krook, Ozan Öktem et al.
Is Retrieval All You Need? Assessment and Emergence of Novelty in Protein Structure Generation
Tongyue Xu, Yijie Zhang, Mutian He et al.