Structural mapping of a chaperone-substrate interaction surface

Callon, Morgane and Burmann, Björn M. and Hiller, Sebastian . (2014) Structural mapping of a chaperone-substrate interaction surface. Angewandte Chemie. International edition in English, Vol. 53, H. 20. pp. 5069-5072.

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Official URL: http://edoc.unibas.ch/dok/A6271944

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NMR spectroscopy is used to detect site-specific intermolecular short-range contacts in a membrane-protein-chaperone complex. This is achieved by an "orthogonal" isotope-labeling scheme that permits the unambiguous detection of intermolecular NOEs between the well-folded chaperone and the unfolded substrate ensemble. The residues involved in these contacts are part of the chaperone-substrate contact interface. The approach is demonstrated for the 70 kDa bacterial Skp-tOmpA complex.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian
Item Type:Article, refereed
Article Subtype:Research Article
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:13 Dec 2017 13:23
Deposited On:18 Jul 2014 09:10

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