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 > Former Organization Units Biozentrum > Structural Biology (Stahlberg) |
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| UniBasel Contributors: | Engel, Andreas H and Stahlberg, Henning |
| Item Type: | Article, refereed |
| Article Subtype: | Research Article |
| Publisher: | Springer |
| ISSN: | 1432-1017 |
| Note: | Publication type according to Uni Basel Research Database: Journal article |
| Related URLs: | |
| Identification Number: |
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| Last Modified: | 08 Jun 2012 06:45 |
| Deposited On: | 22 Mar 2012 13:30 |
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