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Atomic force microscopy for the study of membrane proteins
Authors:Fotiadis Dimitrios
Affiliation:Institute of Biochemistry and Molecular Medicine, and Swiss National Centre of Competence in Research TransCure, University of Bern, CH-3012 Bern, Switzerland. dimitrios.fotiadis@ibmm.unibe.ch
Abstract: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.
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