| Literature DB >> 27511025 |
Benesh Joseph1, Victor M Tormyshev2,3, Olga Yu Rogozhnikova2, Dmitry Akhmetzyanov4, Elena G Bagryanskaya2, Thomas F Prisner5.
Abstract
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.Entities:
Keywords: EPR; PELDOR or DEER; membrane proteins; spin labeling; trityl
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Year: 2016 PMID: 27511025 DOI: 10.1002/anie.201606335
Source DB: PubMed Journal: Angew Chem Int Ed Engl ISSN: 1433-7851 Impact factor: 15.336