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Cloning, expression, purification, and characterization of the membrane protein UncI from Escherichia coli

Hartmann, C. and Engel, A.. (2011) Cloning, expression, purification, and characterization of the membrane protein UncI from Escherichia coli. Protein expression and purification, Vol. 79, H. 2. pp. 187-190.

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Official URL: http://edoc.unibas.ch/dok/A6002467

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Abstract

The Escherichia coli unc-operon encodes the genes for the subunits of the F0F1-ATP synthase and an integral membrane protein of unknown function called UncI. UncI influences the cell-growth and activity of F0F1, but its exact function is still unknown. The expression level is too low to extract milligram amounts of UncI from E. coli membranes and the existing purification protocol based on methanol/chloroform is not suitable for structural and functional studies. Here we present protocols to increase the expression level, to purify UncI in a detergent where UncI is monodisperse, and we characterize its oligomeric 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
Bibsysno:Link to catalogue
Publisher:Elsevier
ISSN:1096-0279
Note:Publication type according to Uni Basel Research Database: Journal article
Last Modified:11 Oct 2012 15:31
Deposited On:11 Oct 2012 15:16

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