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Unzipping a Membrane
Published online by Cambridge University Press: 14 March 2018
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The atomic force microscope (AFM) is well known for its outstanding spatial resolution, but it is becoming increasingly useful as the instrument for force spectroscopy. In the force spectroscopy mode, the AFM can measure tiny tension forces, in the piconewton (pN) range. Daniel Müller, Wolfgang Baurmeister, and Andreas Engel have used the AFM in both the imaging and force spectroscopy modes to pull proteins out of membranes in a controlled fashion.
Müller et al. used Deinococcus radiodurans, a bacterium best known for its high resistance to radiation (as its Genus name implies), as their test subject. They extracted a highly regular membrane from the bacterium, the hexagonally packed intermediate (HPl) layer. They mounted the HPI on mica, so that the hydrophilic outer surface of the HPI adsorbed strongly to the mica, exposing the hydrophobic inner surface to the silicon nitride AFM stylus.
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- Research Article
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- Copyright © Microscopy Society of America 2000
References
Müller, D.J., Baumeister, W., and Engel, A., Controlled unzipping of a bacterial surface layer with atomic force microscopy, Proc. Nat. Acad. Sci. USA
96:13170-13174, 1999.Google Scholar
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