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Journal Article

Sampling the conformational space of membrane protein surfaces with the AFM


Müller,  D. J.
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Scheuring, S., Müller, D. J., Stahlberg, H., Engel, H. A., & Engel, A. (2002). Sampling the conformational space of membrane protein surfaces with the AFM. European Biophysics Journal with Biophysics Letters, 31(3), 172-178.

Cite as: https://hdl.handle.net/21.11116/0000-0001-1348-9
The atomic force microscope acquires topographs of single native membrane proteins at subnanometer resolution. Owing to the high signal-to-noise ratio, such images allow the conformational space of membrane protein surfaces to be sampled. This is demonstrated by topographs of porin OrnpF, aquaporin-Z, and bacteriorhodopsin, all recorded at a lateral resolution of <7 &ANGS; and a vertical resolution of &SIM;1 &ANGS;. The amplitudes of the domain movements were estimated from a large number of single molecule topographs and the corresponding energy landscapes calculated. To visualize the motion of protein domains, movies were generated by similarity ranking of the observed protein configurations. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00249-001-0197-8.