...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>The journal of physical chemistry, B. Condensed matter, materials, surfaces, interfaces & biophysical >Adsorption of Membrane-Associated Proteins to Lipid Bilayers Studied with an Atomic Force Microscope: Myelin Basic Protein and Cytochrome c
【24h】

Adsorption of Membrane-Associated Proteins to Lipid Bilayers Studied with an Atomic Force Microscope: Myelin Basic Protein and Cytochrome c

机译：用原子力显微镜研究膜相关蛋白对脂质双层的吸附：髓磷脂碱性蛋白和细胞色素c

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Atomic force microscopy was used to study the structure of two membrane-associated proteins adsorbed to various supported phospholipid bilayers in physiological buffer. The aim was (a) to develop a preparation for the investigation of membrane-associated proteins at high resolution under native conditions and (b) to obtain information about the factors that determine the adsorption process and the structure of adsorbed proteins. Therefore, solid-supported membranes were formed on mica by spontaneous vesicle adsorption and spreading. Once a homogeneous, pinhole-free bilayer was formed, solutions containing the proteins at appropriate concentrations were applied. The two positively charged proteins chosen were myelin basic protein (MBP), which plays an essential role in the formation of functional myelin, and cytochrome c. On charged bilayers, MBP applied at concentrations of 0.5-50 μg/mL formed aggregates of defined height (1.9 ± 0.2 nm on negatively and 2.7 ± 0.2 nm on positively charged lipids), which at high concentration covered the entire bilayer. These aggregates are probably monomolecular layers of MBP. On neutral lipid adsorbed MBP formed irregular aggregates. Cytochrome c showed a different adsorption: On negatively charged lipid it formed aggregates of defined, monomolecular height (3.3 ± 0.2 nm). On neutral bilayers small aggregates were observed. On positively charged lipid no adsorption was observed at all. These results indicate that (a) the adsorption of cytomchrome c can be interpreted in terms of a dominating electrostatic interaction; (b) MBP adsorption to lipid bilayers is not exclusively electrostatically driven and depends on the specific lipid bilayer composition; (c) the structure of adsorbed aggregates indicates a strong protein-protein interaction.
机译：原子力显微镜用于研究两种膜相关蛋白在生理缓冲液中吸附到各种支持的磷脂双层上的结构。目的是（a）开发一种在自然条件下以高分辨率研究膜相关蛋白的制剂，（b）获得有关决定吸附过程和吸附蛋白结构的因素的信息。因此，通过自发的囊泡吸附和扩散，在云母上形成了固体支撑膜。一旦形成均匀，无针孔的双层，就应用含有适当浓度蛋白质的溶液。选择的两个带正电荷的蛋白质是髓磷脂碱性蛋白（MBP），它在功能性髓磷脂的形成中起着重要作用，而细胞色素c则起着重要作用。在带电的双层上，以0.5-50μg/ mL的浓度施加的MBP形成了确定高度的聚集体（负电荷为1.9±0.2 nm，带正电荷的脂质为2.7±0.2 nm），高浓度覆盖了整个双层。这些聚集体可能是MBP的单分子层。在中性脂质上吸附的MBP形成不规则的聚集体。细胞色素c表现出不同的吸附：在带负电荷的脂质上，它形成确定的单分子高度（3.3±0.2 nm）的聚集体。在中性双层上观察到小的聚集体。在带正电荷的脂质上根本没有观察到吸附。这些结果表明：（a）细胞色素c的吸附可以用主要的静电相互作用来解释; （b）MBP对脂质双层的吸附并非仅由静电驱动，并且取决于特定的脂质双层组成; （c）吸附的聚集体的结构表明强烈的蛋白质-蛋白质相互作用。

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