Journal article
Structural mapping of a chaperone-substrate interaction surface.
- Callon M Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel (Switzerland).
- Burmann BM
- Hiller S
- 2014-04-05
Published in:
- Angewandte Chemie (International ed. in English). - 2014
NMR spectroscopy
chaperone proteins
membrane proteins
protein ensembles
protein-protein interactions
Binding Sites
Magnetic Resonance Spectroscopy
Molecular Chaperones
Protein Conformation
English
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.
- Language
-
- English
- Open access status
- closed
- Identifiers
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- DOI 10.1002/anie.201310963
- PMID 24700611
- Persistent URL
- https://sonar.ch/global/documents/232265
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