Dynamic nuclear polarization of membrane proteins: covalently bound spin-labels at protein–protein interfaces
| Autor: | Boris Dzikovski, Melanie Rosay, Ann E. McDermott, Shane Pawsey, Jack H. Freed, Marc A. Caporini, Benjamin J. Wylie |
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| Rok vydání: | 2015 |
| Předmět: |
Chemistry
Phosphatidylethanolamines Lipid Bilayers Peripheral membrane protein Intermolecular force Electron Spin Resonance Spectroscopy Gramicidin Analytical chemistry Membrane Proteins Phosphatidylserines Biochemistry Article chemistry.chemical_compound Membrane protein Intramolecular force Membrane fluidity Biophysics Protein Interaction Domains and Motifs Spin Labels Spin label Lipid bilayer Nuclear Magnetic Resonance Biomolecular Spectroscopy |
| Zdroj: | Journal of Biomolecular NMR. 61:361-367 |
| ISSN: | 1573-5001 0925-2738 |
| DOI: | 10.1007/s10858-015-9919-6 |
| Popis: | We demonstrate that dynamic nuclear polarization (DNP) of membrane proteins in lipid bilayers may be achieved using a novel polarizing agent: pairs of spin labels covalently bound to a protein of interest interacting at an intermolecular interaction surface. For gramicidin A, nitroxide tags attached to the N-terminal intermolecular interface region become proximal only when bimolecular channels forms in the membrane. We obtained signal enhancements of 6-fold for the dimeric protein. The enhancement affect was comparable to that of a doubly tagged sample of gramicidin C, with intramolecular spin pairs. This approach could be a powerful and selective means for signal enhancement in membrane proteins, and for recognizing intermolecular interfaces. |
| Databáze: | OpenAIRE |
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