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作 者:LI Xiaodong LI Zongli YAN Jiusheng LI Hui HAN Baoshan HU Kunsheng WANG Aojin
机构地区:[1]Center of Condensed Matter Physics,Institute of Physics,Chinese Academy of Sciences,Beijing 100080,China [2]State Key Laboratory of Magnetism,Institute of Physics,Chinese Academy of Sciences,Beijing 100080,China [3]Photosynthesis Research Center,Institute of Botany,Chinese Academy of Sciences,Beijing 100093,China [4]Institute of Biophysics,Chinese Academy of Sciences,Beijing 100101,China
出 处:《Chinese Science Bulletin》2001年第20期1753-1756,共4页
基 金:This work was supported by the State Key Basic I Research and Development Plan Project (Grant No. 1998010102).
摘 要:The structural change of purple membrane during storage has been investigated by means of transmission electron microscope and atomic force microscope. It is found that many liposomes have spontaneously evolved from the purple membrane sheets isolated three years ago. The membrane proteins on the liposomes, bacteriorhodopsin, are still presented as trimers in 2-D hexagonal structure, which is the same as that in natural cell membrane. However, the cytoplasmic surface of purple membrane faced outside on the liposomes.The structural change of purple membrane during storage has been investigated by means of transmis sion electron microscope and atomic force microscope. It is found that many liposomes have spontaneously evolved from the purple membrane sheets isolated three years ago. The membrane proteins on the liposomes, bacteriorhodopsin, are still presented as trimers in 2-D hexagonal structure, which is the same as that in natural cell membrane. However, the cytoplasmic surface of purple membrane faced outside on the liposomes.
关 键 词:transmission electron MICROSCOPE (TEM) ATOMIC force MICROSCOPE (AFM) PURPLE membrane (PM) BACTERIORHODOPSIN (BR).
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