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Eur Biophys J. 2002 Jun;31(3):172-8. Epub 2002 Jan 29.

Sampling the conformational space of membrane protein surfaces with the AFM.

Author information

1
M.E. Müller Institute for Microscopy at the Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland.

Abstract

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 OmpF, aquaporin-Z, and bacteriorhodopsin, all recorded at a lateral resolution of <7 A and a vertical resolution of ~1 A. 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.

PMID:
12029329
DOI:
10.1007/s00249-001-0197-8
[Indexed for MEDLINE]

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