Protocol abstract
Nature Protocols 2, - 2191 - 2197 (2007)
Published online: 6 September 2007 | doi:10.1038/nprot.2007.309
Subject Categories: Imaging | Isolation, purification and separation | Spectroscopy and structural analysis | Biochemistry and protein analysis
Atomic force microscopy and spectroscopy of native membrane proteins
Daniel J Müller1 & Andreas Engel2
Abstract
Membrane proteins comprise 30% of the proteome of higher organisms. They mediate energy conversion, signal transduction, solute transport and secretion. Their native environment is a bilayer in a physiological buffer solution, hence their structure and function are preferably assessed in this environment. The surface structure of single membrane proteins can be determined in buffer solutions by atomic force microscopy (AFM) at a lateral resolution of less than 1 nm and a vertical resolution of 0.1–0.2 nm. Moreover, single proteins can be directly addressed, stuck to the AFM stylus and subsequently unfolded, revealing the molecular interactions of the protein studied. The examples discussed here illustrate the power of AFM in the structural analysis of membrane proteins in a native environment.
- Center of Biotechnology, University of Technology, Tatzberg 47-51, Dresden, Germany.
- M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland.
Correspondence to: Andreas Engel2 e-mail: andreas.engel@unibas.ch
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