首页> 外文会议>International symposium on bioanalytical chemistry >STRUCTURAL ANALYSIS OF THE NICOTINIC-ACETYLCHOLINE RECEPTOR IMMOBILIZED ON CRYSTALS AND PHOSPHOLIPIDES STUDIED BY FTIR-SPECTROSCOPY
【24h】

STRUCTURAL ANALYSIS OF THE NICOTINIC-ACETYLCHOLINE RECEPTOR IMMOBILIZED ON CRYSTALS AND PHOSPHOLIPIDES STUDIED BY FTIR-SPECTROSCOPY

机译:用FTIR光谱研究固定在晶体和磷脂上的烟碱 - 乙酰胆碱受体的结构分析

获取原文

摘要

The n-Acetylcholine Receptor (n-AChR) is a transmembrane protein which is involved in chemo-electrical signal transduction across postsynaptic membranes and neuromuscular junctions. This receptor is one of the best characterized for ligand gated ion channels [1]. In order to study its function by FTIR spectroscopy outside its natural media receptor containing membranes have to be immobilized directly on crystals [2]. This technique has already been successfully applied to other integral membrane proteins like bacteriorhodopsin [3]. In this study we present evidence for the proper orientation of membranes containing n-AChR on crystals. Orientation on phospholipid surfaces is also investigated.
机译:N-乙酰胆碱受体(N-ACHR)是跨膜蛋白,其参与突触后膜和神经肌肉连接点的化疗电信号转导。该受体是对配体栅极离子通道的最佳特征之一[1]。为了通过FTIR光谱研究其天然介质受体的FTIR光谱,必须将膜直接固定在晶体上[2]。该技术已经成功地应用于其他整体膜蛋白,如细菌磷脂[3]。在这项研究中,我们提出了含有N-ACHR上晶体的适当取向的证据。还研究了磷脂表面的取向。

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