Single-molecule studies of membrane proteins

Muller, D. J. and Sapra, K. T. and Scheuring, S. and Kedrov, A. and Frederix, P. L. and Fotiadis, D. and Engel, A.. (2006) Single-molecule studies of membrane proteins. Current Opinion in Structural Biology, Vol. 16, H. 4. pp. 489-495.

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Official URL: http://edoc.unibas.ch/dok/A5262429

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Characterizing membrane proteins with single-molecule techniques provides structural and functional insights that cannot be obtained with conventional approaches. Recent studies show that atomic force microscopy (AFM) in the context of a 'lab on a tip' enables the measurement of multiple parameters of membrane proteins. This multifunctional tool can be applied to probe the oligomeric states and conformational changes of membrane protein assemblies in their native environment. The ability to determine diverse properties at high spatial resolution facilitates the mapping of structural flexibilities, electrostatic potentials and electric currents. By using the AFM tip as tweezer, it is possible to characterize unfolding and refolding pathways of single proteins and the location of their molecular interactions. These interactions dictate the stability of the protein and might be modulated by ligands that alter the protein's functional state.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel)
UniBasel Contributors:Engel, Andreas H
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Current Biology
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:22 Mar 2012 14:22
Deposited On:22 Mar 2012 13:31

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