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去垢剂在膜蛋白研究中的应用 被引量:2

Applications of Detergents in Membrane Proteins Research
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摘要 去垢剂是同时具有亲水极性基团和疏水非极性基团的双极性分子,能够使脂膜解体释放膜蛋白,并在溶液中为去膜状态下的膜蛋白提供疏水环境,维持和保护膜蛋白的疏水跨膜结构,在膜蛋白的结构和功能研究中有重要的意义。去垢剂的双极性和理化特性,如临界胶束浓度能够极大影响去垢剂和膜蛋白间的相互作用。在膜蛋白研究中,需要充分利用去垢剂的结构和特性:一方面,需要利用去垢剂代替脂质分子支持和稳定去膜状态下膜蛋白的结构和功能;另一方面,需要控制去垢剂和膜蛋白的相互作用,以满足膜蛋白结构研究如蛋白质结晶试验的要求。简要介绍了去垢剂在膜蛋白研究中的最新应用进展,涉及去垢剂在膜蛋白离体表达、分离和纯化、以及结构研究中的应用。 Detergents are amphiphilic molecules and able to solubilisc membrane proteins from lipid membranes and provide hydrophobic protection for membrane proteins in hydrophilic solutions. Resultant detergent-solubilized membrane proteins can maintain their native trans-membrane structure in lipid-free environments. Therefore, detergents are valuable in structural and functional characterizations of membrane proteins. Interactions between detergents and membrane proteins are affected by the amphiphilic features together with the physical and the chemical properties of detergents, such as critical Micelle concentration. The research on membrane proteins requires investigators to make full use of these special characteristics of detergents. On the one hand ,one can use detergents instead of lipid molecules to stabilize and maintain the structure and activity of lipid-free membrane proteins;on the other hand, one needs to control interactions between detergents and membrane proteins for structural investigations on membrane proteins using techniques such as protein crystallization. In this article, the latest bibliography were reviewed related to applications of detergents to in vitro expression, purification, and structural investigation of membrane proteins.
出处 《生物技术通报》 CAS CSCD 北大核心 2010年第2期205-212,共8页 Biotechnology Bulletin
基金 国家自然科学基金(30600004) 教育部留学回国人员科研启动基金资助项目
关键词 去垢剂 膜蛋白 离体表达 纯化 蛋白质结构 Detergents Membrane proteins in vitro expression Purification Protein structure
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  • 2Shi CW,Shao W,Xiong Y, et al. A gas chromatographic method for quantification of detergents frequently used in membrane protein structural studies. Analytical Biochemistry,2008,383 (2) :326-328.
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