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

doi:10.1016/S0014-5793(02)03444-0

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

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	133-138
Number of pages	6
Journal	FEBS Letters
Volume	530
Issue number	1-3
DOIs	https://doi.org/10.1016/S0014-5793(02)03444-0
Publication status	Published - 2002 Oct 23
Externally published	Yes

Keywords

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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10.1016/S0014-5793(02)03444-0

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

abstract = "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.",

keywords = "Branched chain α-ketoacid dehydrogenase, Lipoyl-bearing domain, Maple syrup urine disease, Protein folding, Stopped flow kinetics",

author = "Naik, {Mandar T.} and Chang, {Yu Chu} and Huang, {Tai huang}",

note = "Funding Information: We thank Jacinta L. Chuang and Dr. David T. Chuang for providing the hbLBD clone and for stimulating discussions. This project is supported by a grant from the National Science Council of the Republic of China (NSC90-2113-M-001-023). ",

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doi = "10.1016/S0014-5793(02)03444-0",

language = "English",

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journal = "FEBS Letters",

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T1 - Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain α-ketoacid dehydrogenase complex

AU - Naik, Mandar T.

AU - Chang, Yu Chu

AU - Huang, Tai huang

N1 - Funding Information: We thank Jacinta L. Chuang and Dr. David T. Chuang for providing the hbLBD clone and for stimulating discussions. This project is supported by a grant from the National Science Council of the Republic of China (NSC90-2113-M-001-023).

PY - 2002/10/23

Y1 - 2002/10/23

N2 - 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.

AB - 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.

KW - Branched chain α-ketoacid dehydrogenase

KW - Lipoyl-bearing domain

KW - Maple syrup urine disease

KW - Protein folding

KW - Stopped flow kinetics

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DO - 10.1016/S0014-5793(02)03444-0

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AN - SCOPUS:0037163881

SN - 0014-5793

VL - 530

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JO - FEBS Letters

JF - FEBS Letters

IS - 1-3

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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