AI Article Synopsis
- The study introduces a new method for enhancing nuclear polarization in membrane proteins using pairs of covalently bound spin labels that interact on the protein's surface.
- The researchers demonstrated this technique with gramicidin A, achieving a sixfold signal enhancement when the protein formed bimolecular channels in the lipid membrane.
- This approach offers a selective way to enhance signals in membrane proteins and identify intermolecular interaction areas, showing results comparable to existing tagging methods.
Article 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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4819240 | PMC |
| http://dx.doi.org/10.1007/s10858-015-9919-6 | DOI Listing |
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