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Progress in the analysis of membrane protein structure and function

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de Groot,  B. L.
Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Grubmueller,  H.
Research Group of Theoretical Molecular Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Werten, P. J. L., Remigy, H. W., de Groot, B. L., Fotiadis, D., Philippsen, A., Stahlberg, H., et al. (2002). Progress in the analysis of membrane protein structure and function. FEBS Letters, 529(1), 65-72. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T36-46MJRV5-6-C&_cdi=4938&_user=38661&_pii=S0014579302032908&_orig=search&_coverDate=10%2F02%2F2002&_sk=994709998&view=c&wchp=dGLzVlb-zSkWA&md5=3171a73d64b9eafeff295fa593c42bb8&ie=/sdarticle.pdf.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F2CC-E
Abstract
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 subnanometer resolution, and their conformational states to be sampled. This review summarizes the steps in membrane protein structure determination and illuminates recent progress. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.