Atomic force microscopy for the study of membrane proteins

被引:32
|
作者
Fotiadis, Dimitrios [1 ,2 ]
机构
[1] Univ Bern, Inst Biochem & Mol Med, CH-3012 Bern, Switzerland
[2] Univ Bern, Swiss Natl Ctr Competence Res NCCR TransCure, CH-3012 Bern, Switzerland
基金
瑞士国家科学基金会;
关键词
PHOTOSYNTHETIC MEMBRANES; BIOMOLECULAR PROCESSES; CONFORMATIONAL-CHANGES; NATIVE MEMBRANE; RHODOPSIN; CHANNEL; BACTERIORHODOPSIN; ORGANISMS; CRYSTALS; VOLTAGE;
D O I
10.1016/j.copbio.2011.11.032
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Fundamental biological processes such as cell-cell communication, signal transduction, molecular transport and energy conversion are performed by membrane proteins. These important proteins are studied best in their native environment, the lipid bilayer. The atomic force microscope (AFM) is the instrument of choice to determine the native surface structure, supramolecular organization, conformational changes and dynamics of membrane-embedded proteins under near-physiological conditions. In addition, membrane proteins are imaged at subnanometer resolution and at the single molecule level with the AFM. This review highlights the major advances and results achieved on reconstituted membrane proteins and native membranes as well as the recent developments of the AFM for imaging.
引用
收藏
页码:510 / 515
页数:6
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