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Sampling the conformational space of membrane protein surfaces with the AFM

Scheuring, S. and Muller, D. J. and Stahlberg, H. and Engel, H. -A. and Engel, A.. (2002) Sampling the conformational space of membrane protein surfaces with the AFM. European biophysics journal, Vol. 31, H. 3. pp. 172-178.

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Official URL: http://edoc.unibas.ch/dok/A5257651

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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
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
UniBasel Contributors:Engel, Andreas H and Stahlberg, Henning
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Springer
ISSN:1432-1017
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:08 Jun 2012 06:45
Deposited On:22 Mar 2012 13:30

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