Macromolecular and Small Molecular Crowding Have Similar Effects on alpha-Synuclein Structure

CORC > 武汉物理与数学研究所 > 中国科学院武汉物理与数学研究所 > 磁共振基础研究部

	Macromolecular and Small Molecular Crowding Have Similar Effects on alpha-Synuclein Structure
	Bai, Jia 1,2; Liu, Maili 1; Pielak, Gary J.3; Li, Conggang 1
刊名	CHEMPHYSCHEM
	2017
卷号	18 期号:1 页码:55-58
关键词	circular dichroism macromolecular crowding NMR spectroscopy protein structure alpha-synuclein
英文摘要	The intracellular milieu contains upwards of 400 g of macromolecules per liter. This crowding is thought to have a larger influence on intrinsically disordered proteins, whose chains are expanded, than on compact globular proteins. Classic theories of macromolecular crowding predict that increasing excluded volume effects will lead disordered proteins to compaction, and a great deal of data, from both simulation and experiments support this idea. We used nuclear magnetic resonance, circular dichroism, and fluorescence spectroscopies to characterize the structure and fibrillation of alpha-synuclein, an intrinsically disordered protein implicated in Parkinson's disease, using Ficoll70, its monomer sucrose and bovine serum albumin as crowding agents. Surprisingly, volume exclusion induced by high concentrations of macromolecules may not be the main reason for the compaction of alpha-synuclein. Our results indicate that all aspects crowding must be considered to understand protein conformation under crowded conditions.
WOS标题词	Science & Technology ; Physical Sciences
类目[WOS]	Chemistry, Physical ; Physics, Atomic, Molecular & Chemical
研究领域[WOS]	Chemistry ; Physics
关键词[WOS]	PARAMAGNETIC RELAXATION ENHANCEMENT ; INTRINSICALLY DISORDERED PROTEINS ; SECONDARY STRUCTURE ; THIOFLAVIN-T ; PARKINSONS-DISEASE ; NMR-SPECTROSCOPY ; FIBRIL FORMATION ; AMYLOID FIBRILS ; UNFOLDED STATE ; CHEMICAL-SHIFT
收录类别	SCI
语种	英语
WOS记录号	WOS:000393190100010
内容类型	期刊论文
源URL	[http://ir.wipm.ac.cn/handle/112942/10033]
专题	武汉物理与数学研究所_磁共振基础研究部
作者单位	1.Chinese Acad Sci, Wuhan Inst Phys & Math, Natl Ctr Magnet Resonance Wuhan, Key Lab Magnet Resonance Biol Syst,State Key Lab, Wuhan 430071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing, Peoples R China 3.Univ N Carolina, Dept Biochem & Biophys, Dept Chem, Chapel Hill, NC 27599 USA
推荐引用方式 GB/T 7714	Bai, Jia,Liu, Maili,Pielak, Gary J.,et al. Macromolecular and Small Molecular Crowding Have Similar Effects on alpha-Synuclein Structure[J]. CHEMPHYSCHEM,2017,18(1):55-58.
APA	Bai, Jia,Liu, Maili,Pielak, Gary J.,&Li, Conggang.(2017).Macromolecular and Small Molecular Crowding Have Similar Effects on alpha-Synuclein Structure.CHEMPHYSCHEM,18(1),55-58.
MLA	Bai, Jia,et al."Macromolecular and Small Molecular Crowding Have Similar Effects on alpha-Synuclein Structure".CHEMPHYSCHEM 18.1(2017):55-58.