Dynamic nuclear polarization of membrane proteins: covalently bound spin-labels at protein-protein interfaces.
J Biomol NMR
; 61(3-4): 361-7, 2015 Apr.
Article
en En
| MEDLINE
| ID: mdl-25828256
ABSTRACT
We demonstrate that dynamic nuclear polarization 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 sixfold for the dimeric protein. The enhancement effect 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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Resonancia Magnética Nuclear Biomolecular
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Gramicidina
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Proteínas de la Membrana
Idioma:
En
Año:
2015
Tipo del documento:
Article