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          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: Publikationen mpi-cbg 2003     Display Documents

ID: 15468.0, MPI für molekulare Zellbiologie und Genetik / Publikationen mpi-cbg 2003
Sampling the conformational space of membrane protein surfaces with the AFM
Authors:Scheuring, S.; Müller, D. J.; Stahlberg, H.; Engel, H. A.; Engel, A.
Date of Publication (YYYY-MM-DD):2002-06
Title of Journal:European Biophysics Journal with Biophysics Letters
Journal Abbrev.:Eur. Biophys. J. Biophys. Lett.
Issue / Number:3
Start Page:172
End Page:178
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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.
Free Keywords:loops; beta-turns; membrane protein; two-dimensional crystal; energy landscape
Comment of the Author/Creator:Date: 2002, JUN
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für molekulare Zellbiologie und Genetik
External Affiliations:Univ Basel, Biozentrum, ME Muller Inst Microscopy, Klingelbergstr 70, CH-4056 Basel, Switzerland; Univ Basel, Dept Phys & Astron, CH-4056 Basel, Switzerland
Identifiers:ISI:000176827900002 [ID No:1]
ISSN:0175-7571 [ID No:2]
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