Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 55, Issue 38, Pages 11538-11542Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201606335
Keywords
EPR; membrane proteins; PELDOR or DEER; spin labeling; trityl
Categories
Funding
- Deutsche Forschungsgemeinschaft [SFB 807]
- Russian Science Foundation [14-14-00922]
- Russian Foundation for Basic Research [14-03-93180]
- Russian Science Foundation [14-14-00922] Funding Source: Russian Science Foundation
Ask authors/readers for more resources
The orchestrated interaction of transmembrane proteins with other molecules mediates several crucial biological processes. Detergent solubilization may significantly alter or even abolish such hetero-oligomeric interactions, which makes observing them at high resolution in their native environment technically challenging. Dipolar electron paramagnetic resonance (EPR) techniques such as pulsed electro-electron double resonance (PELDOR) can provide very precise distances within biomolecules. To concurrently determine the inter-subunit interaction and the intra-subunit conformational changes in hetero-oligomeric complexes, a combination of different spin labels is required. Orthogonal spin labeling using a triarylmethyl (TAM) label in combination with a nitroxide label is used to detect protein-ligand interactions in native lipid bilayers. This approach provides a higher sensitivity and total selectivity and will greatly facilitate the investigation of multimeric transmembrane complexes employing different spin labels in the native lipid environment.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available