Atomic force microscopy for the study of membrane proteins

Fotiadis, Dimitrios (2012). Atomic force microscopy for the study of membrane proteins. Current opinion in biotechnology, 23(4), pp. 510-5. Amsterdam: Elsevier 10.1016/j.copbio.2011.11.032

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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.

Item Type:	Journal Article (Further Contribution)
Division/Institute:	04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine
UniBE Contributor:	Fotiadis, Dimitrios José
ISSN:	0958-1669
Publisher:	Elsevier
Language:	English
Submitter:	Factscience Import
Date Deposited:	04 Oct 2013 14:37
Last Modified:	05 Dec 2022 14:11
Publisher DOI:	10.1016/j.copbio.2011.11.032
PubMed ID:	22176750
Web of Science ID:	000308266100003
URI:	https://boris.unibe.ch/id/eprint/15048 (FactScience: 222202)