期刊
JOURNAL OF BIOMOLECULAR NMR
卷 61, 期 3-4, 页码 361-367出版社
SPRINGER
DOI: 10.1007/s10858-015-9919-6
关键词
Dynamic nuclear polarization; DNP; Membrane proteins; Solid-state NMR; Gramicidin; DEER spectroscopy
资金
- National Institutes of Health
- National Science Foundation
- New York State Office of Science, Technology, and Academic Research
- NIH [P41 GM66354, R01 GM 88724]
- NSF MCB [0749381]
- NIH NRSA [F32 087908]
- NIH/NIGMS [P41GM103521]
- NIH/NIBIB [R01EB003150]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1412253] Funding Source: National Science Foundation
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0749381] Funding Source: National Science Foundation
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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