Biophysical studies on the full-length human cyclin A(2): Protein stability and folding/unfolding thermodynamics

doi:10.1021/jp712026m

IMR OpenIR

	Biophysical studies on the full-length human cyclin A(2): Protein stability and folding/unfolding thermodynamics
	Wang, Xiaohui; Ren, Jinsong; Qu, Xiaogang
通讯作者	Qu, Xiaogang(xqu@ciac.jl.cn)
	2008-07-17
发表期刊	JOURNAL OF PHYSICAL CHEMISTRY B
ISSN	1520-6106
卷号	112 期号:28 页码:8346-8353
摘要	Human cyclin A(2) participates in cell cycle regulation, DNA replication, and transcription. Its overexpression has been implicated in the development and progression of a variety of human cancers. However, cyclin A(2) or its truncated form is very unstable in the absence of binding partner, which makes it difficult to get a deep insight of structural basis of the interactions. Therefore, biophysical studies of the full-length human cyclin A, would provide important information regarding protein stability and folding/unfolding process. To the best of our knowledge, these have not been reported. In this report, we found that cyclin A(2) stability depended on pH, salt concentration, and denaturant concentration, and low concentration denaturant increased cyclin A, stability studied by UV melting, fluorescence spectroscopy, limited proteolysis, and circular dichroism. The thermal unfolding/folding process could be described by Lumry-Eyring model: N <-> I -> D, followed by decreasing alpha-helix content and forming intermolecular antiparallel pleated beta-sheet structures in the aggregate. Our results are of importance for studying the interactions between cyclin A(2) and therapeutic agents, such as small molecules or peptides, because cyclin A(2) is very unstable in the absence of its biological associated kinases.
DOI	10.1021/jp712026m
收录类别	SCI
语种	英语
WOS研究方向	Chemistry
WOS类目	Chemistry, Physical
WOS记录号	WOS:000257542500017
出版者	AMER CHEMICAL SOC
引用统计	被引频次：11[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.imr.ac.cn/handle/321006/94585
专题	中国科学院金属研究所
通讯作者	Qu, Xiaogang
作者单位	Chinese Acad Sci, Changchun Inst Appl Chem, Div Biol Inorgan Chem,Key Lab Rare Earth Chem & P, Grad Sch Chinese Acad Sci, Changchun 130022, Jilin, Peoples R China
推荐引用方式 GB/T 7714	Wang, Xiaohui,Ren, Jinsong,Qu, Xiaogang. Biophysical studies on the full-length human cyclin A(2): Protein stability and folding/unfolding thermodynamics[J]. JOURNAL OF PHYSICAL CHEMISTRY B,2008,112(28):8346-8353.
APA	Wang, Xiaohui,Ren, Jinsong,&Qu, Xiaogang.(2008).Biophysical studies on the full-length human cyclin A(2): Protein stability and folding/unfolding thermodynamics.JOURNAL OF PHYSICAL CHEMISTRY B,112(28),8346-8353.
MLA	Wang, Xiaohui,et al."Biophysical studies on the full-length human cyclin A(2): Protein stability and folding/unfolding thermodynamics".JOURNAL OF PHYSICAL CHEMISTRY B 112.28(2008):8346-8353.