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 ΔGH2O and m obtained from the kinetic analysis are consistent with the equilibrium measurements.
原文 | 英語 |
---|---|
頁(從 - 到) | 133-138 |
頁數 | 6 |
期刊 | FEBS Letters |
卷 | 530 |
發行號 | 1-3 |
DOIs | |
出版狀態 | 已發佈 - 10月 23 2002 |
ASJC Scopus subject areas
- 生物物理學
- 結構生物學
- 生物化學
- 分子生物學
- 遺傳學
- 細胞生物學