...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Tools To Fold Integral Membrane Proteins to Their Active Form
【24h】

Tools To Fold Integral Membrane Proteins to Their Active Form

机译：将整合膜蛋白折叠成活性形式的工具

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Among the major obstacles to pharmacological and structural studies of integral membrane proteins (MPs)are their natural scarcity and the difficulty in overproducing them in their native form.MPs can be overexpressed in the non-native state as inclusion bodies,but inducing them to achieve their functional three-dimensional structure has proven to be a major challenge.We describe here the use of an amphipathic polymer,amphipol A8-35,as a novel environment that allows both beta-barrel and alpha-helical MPs to fold to their native state,in the absence of detergents or lipids.Amphipols,which are extremely mild surfactants,appear to favor the formation of native intramolecular protein-protein interactions over intermolecular or protein-surfactant ones.The feasibility of the approach is demonstrated using as models OmpA and FomA,two outer membrane proteins from the eubacteria Escherichia coli and Fusobacterium nucleatum,respectively,and bacteriorhodopsin,a light-driven proton pump from the plasma membrane of the archaebacterium Halobacterium salinarium.
机译：整体膜蛋白（MPs）的药理和结构研究的主要障碍之一是它们的天然稀缺性和以天然形式过量生产它们的困难.MPs可以在非天然状态下以包涵体的形式过表达，但会诱导它们实现它们的功能性三维结构已被证明是一个重大挑战。我们在此描述使用两亲性聚合物amphipol A8-35作为一种新颖的环境，该环境可同时使β-桶形和α-螺旋MP折叠到其原始状态，是非常温和的表面活性剂，两性分子似乎比分子间或蛋白质表面活性剂更倾向于形成天然的分子内蛋白质-蛋白质相互作用。使用OmpA和FomA模型证明了该方法的可行性，分别来自真细菌大肠埃希菌和核梭菌的两种外膜蛋白，以及细菌视紫红质，一种来自p的光驱动质子泵盐杆菌盐杆菌的膜。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号