Folding of the Protein Domain hbSBD

Details Folding of the Protein Domain hbSBD Folding of the Protein Domain hbSBD

2006-12-17

arxiv.org/abs/q-bio/0612031v1

Biophysical J. 89, 3353 (2005)

Biology

Quantitative Biology

Biomolecules

25 pages, 7 figures, 1 table, published in Biophysical Journal

Scientific paper

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.

Affiliated with

Also associated with

No associations

Rating

Folding of the Protein Domain hbSBD does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Folding of the Protein Domain hbSBD, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Folding of the Protein Domain hbSBD will most certainly appreciate the feedback.

Rate now

Comments { 0 }

Profile ID: LFWR-SCP-O-609553