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

FEBS Letters

Huang, Tai-huang¹  Naik, Mandar T¹  Chang, Yu-Chu¹ 

[1] Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan

关键词: Protein folding;    Lipoyl-bearing domain;    Branched chain α-ketoacid dehydrogenase;    Maple syrup urine disease;    Stopped flow kinetics;   

DOI  :  10.1016/S0014-5793(02)03444-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 ΔG H₂O and m obtained from the kinetic analysis are consistent with the equilibrium measurements.

【 授权许可】

Unknown