Reversible folding of cysteine-rich metallothionein by an overcritical reaction path

Yi Liang Liu, Hui Ting Lee, Chia-Ching Chang, Lou Sing Kan*

*此作品的通信作者

研究成果: Article同行評審

15 引文 斯高帕斯(Scopus)

摘要

A first-order-like state transition is considered to be involved in the restoration of the activities of a few proteins by correctly folding the protein [Phys. Rev. E 66 (2002) 021903]. In order to understand the general applicability of this mechanism, we studied a metallothionein (MT) protein with an unconventional structure, i.e., without any α-helix or β-sheet. MT is a 61 amino-acid peptide. There are 6-7 Zn2+ ions, which bind avidly to 20 conserved cysteines (Cys) of MT. These properties indicate that the structure of MT is quite different from those of the other proteins. Similar to our previous findings, the denatured MT can be folded without any aggregation via a designated stepwise quasi-static process (an over-critical reaction path). The particle size of folded MT intermediates, determined by dynamic light scattering, shrank right after the first folding stage. It is consistent with a collapse-model. In addition, results from both atomic absorption and circular dichroism (CD) indicate that the stable intermediates may fold to the native conformation but with only partial Zn2+ binding, which in turn implies that those folding intermediates are in a molten globular state. These reversible unfolding and folding processes indicate that Cys-rich protein, MT, may also be folded by way of a first-order-like state transition mechanism. We suspect that this process may likely be involved in the reaction of the metal substitution process in metal containing enzymes.

原文English
頁(從 - 到)59-63
頁數5
期刊Biochemical and Biophysical Research Communications
306
發行號1
DOIs
出版狀態Published - 20 6月 2003

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