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Published online by Cambridge University Press: 14 March 2018
Proteins in biologic membranes perform a large variety of essential functions. The fact that about one third of all genes code for membrane proteins, and that the majority of drugs target these proteins, attest to that fact. However, until now, proteins have been studied under artificial conditions, such as after being crystallized, frozen, or adsorbed to a substrate. Rui Pedro Gonçalves, Guillaume Agnus, Pierre Sens, Christine Houssin, Bernard Bartenlian, and Simon Scheuring have devised a novel setup with the atomic force microscope (AFM) to allow proteins to be probed while they are in unsupported membranes. Their method is similar in principle to methods where a small area of a membrane is sampled, such as when a piece of membrane is examined by patch clamping. The difference is that instead of attaching a membrane to the end of a pipette, it is spread across a piece of perforated Si(001).
The author gratefully acknowledges Dr. Simon Scheuring for reviewing this article.
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3. Gonçalves, R.P., and Scheuring, S., Manipulating and imaging individual membrane proteins by AFM, Surface and Interface Analysis 38:1413–1418, 2006.CrossRefGoogle Scholar
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