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• W2010599420 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." @default.
• W2010599420 created "2016-06-24" @default.
• W2010599420 creator A5021120268 @default.
• W2010599420 date "2012-08-01" @default.
• W2010599420 modified "2023-09-26" @default.
• W2010599420 title "Atomic force microscopy for the study of membrane proteins" @default.
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• W2010599420 doi "https://doi.org/10.1016/j.copbio.2011.11.032" @default.
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