Progress in the analysis of membrane protein structure and function

Werten, P. J. L. and Rémigy, H. W. and de Groot, B. L. and Fotiadis, D. and Philippsen, A. and Stahlberg, H. and Grubmüller, H. and Engel, A.. (2002) Progress in the analysis of membrane protein structure and function. FEBS letters, Vol. 529, H. 1. pp. 65-72.

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Official URL: http://edoc.unibas.ch/dok/A5257649

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Structural information on membrane proteins is sparse, yet they represent an important class of proteins that is encoded by about 30% of all genes. Progress has primarily been achieved with bacterial proteins, but efforts to solve the structure of eukaryotic membrane proteins are also increasing. Most of the structures currently available have been obtained by exploiting the power of X-ray crystallography. Recent results, however, have demonstrated the accuracy of electron crystallography and the imaging power of the atomic force microscope. These instruments allow membrane proteins to be studied while embedded in the bi-layer, and thus in a functional state. The low signal-to-noise ratio of cryo-electron microscopy is overcome by crystallizing membrane proteins in a two-dimensional protein-lipid membrane, allowing its atomic structure to be determined. In contrast, the high signal-to-noise ratio of atomic force microscopy allows individual protein surfaces to be imaged at sub-nanometer resolution, and their conformational states to be sampled. This review summarizes the steps in membrane protein structure determination and illuminates recent progress.
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
Publisher:Elsevier Science
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 13:18

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