Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain α-ketoacid dehydrogenase complex

Mandar T. Naik, Yu Chu Chang, Tai huang Huang

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4 Citations (Scopus)


A reversible two-step (native state↔denatured state) folding mechanism based on equilibrium and stopped flow experiments is proposed for urea denaturation of the lipoyl-bearing domain (hbLBD) of human mitochondrial branched chain α-ketoacid dehydrogenase (BCKD) complex. The results from this circular dichroism (CD) and fluorescence study have ruled out populated kinetic or equilibrium intermediates on folding pathway of this β-barrel domain under experimental conditions. Both studies suggested mono-exponential kinetics without any burst phases. Moreover the thermodynamic parameters ΔGH2O and m obtained from the kinetic analysis are consistent with the equilibrium measurements.

Original languageEnglish
Pages (from-to)133-138
Number of pages6
JournalFEBS Letters
Issue number1-3
Publication statusPublished - 2002 Oct 23



  • Branched chain α-ketoacid dehydrogenase
  • Lipoyl-bearing domain
  • Maple syrup urine disease
  • Protein folding
  • Stopped flow kinetics

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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