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Folding kinetics of the lipoic acid‐bearing domain of human mitochondrial branched chain α‐ketoacid dehydrogenase complex
Author(s) -
Naik Mandar T,
Chang Yu-Chu,
Huang Tai-huang
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03444-0
Subject(s) - kinetics , chemistry , folding (dsp implementation) , protein folding , equilibrium unfolding , circular dichroism , dehydrogenase , denaturation (fissile materials) , stereochemistry , biophysics , enzyme , biochemistry , biology , physics , quantum mechanics , electrical engineering , nuclear chemistry , engineering
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 Δ G H 2 O and m obtained from the kinetic analysis are consistent with the equilibrium measurements.