Folding kinetics of the lipoic acid-bearing domain of human mitochondrial branched chain alpha-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 alpha-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 beta-barrel domain under experimental conditions. Both studies suggested mono-exponential kinetics without any burst phases. Moreover the thermodynamic parameters DeltaG(H(2)O) and m obtained from the kinetic analysis are consistent with the equilibrium measurements.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Naik MT,Chang YC,Huang TH

doi

10.1016/s0014-5793(02)03444-0

keywords:

subject

Has Abstract

pub_date

2002-10-23 00:00:00

pages

133-8

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302034440

journal_volume

530

pub_type

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