期刊
CHEMISTRY-AN ASIAN JOURNAL
卷 9, 期 2, 页码 632-638出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/asia.201301303
关键词
amphiphiles; membrane proteins; molecular design; protein solubilization; protein stabilization
资金
- Korean government (MSIP) [2008-0061891, 2012R1A1A1040964]
Membrane proteins are inherently amphipathic and undergo dynamic conformational changes for proper function within native membranes. Maintaining the functional structures of these biomacromolecules in aqueous media is necessary for structural studies but difficult to achieve with currently available tools, thus necessitating the development of novel agents with favorable properties. This study introduces several new glucose-neopentyl glycol (GNG) amphiphiles and reveals some agents that display favorable behaviors for the solubilization and stabilization of a large, multi-subunit membrane protein assembly. Furthermore, a detergent structure-property relationship that could serve as a useful guideline for the design of novel amphiphiles is discussed.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据