title: Atomic force microscopy for the study of membrane proteins.
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.
authors.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
authors.forename: Dimitrios
authors.initials: D
authors.lastname: Fotiadis
mesh_terms: D000818:Animals; D001419:Bacteria / Q000737:chemistry; D056890:Eukaryota / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D018625:Microscopy, Atomic Force / Q000379:methods*; D036103:Nanotechnology / Q000379:methods
chemical_list: D008051:Lipid Bilayers; D008565:Membrane Proteins