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 Lettjournal_title
FEBS lettersauthors
Naik MT,Chang YC,Huang THdoi
10.1016/s0014-5793(02)03444-0keywords:
subject
Has Abstractpub_date
2002-10-23 00:00:00pages
133-8issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302034440journal_volume
530pub_type
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