Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 24, Pages 8255-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja102932n
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Funding
- NSF [MCB 0843520]
- North Carolina Biotechnology Center
- National Institutes of Health
- [P41EB002031]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0843520] Funding Source: National Science Foundation
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A general sequential assignment strategy for uniformly N-15-labeled uniaxially aligned membrane proteins is proposed. Mismatched Hartmann-Hahn magnetization transfer is employed to establish proton-mediated correlations among the neighboring N-15 backbone spins. Magnetically aligned Pf1 phage coat protein was used to illustrate the method. Exchanged and nonexchanged separated local field spectra were acquired and overlaid to distinguish the cross-peaks from the main peaks. Most of the original assignments from the literature were confirmed without selectively labeled samples. This method is applicable to proteins with arbitrary topology and will find use in assigning solid-state NMR spectra of oriented membrane proteins for their subsequent structure determination.
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