期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 141, 期 14, 页码 5681-5691出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.8b09216
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资金
- National Science Foundation (NSF) [CHE-1708773, CHE-0959496]
- National Institutes of Health (NIGMS) [P50 GM082251]
- National Institutes of Health (NIAID) [P50 GM082251]
- National Institutes of Health (NIH) [P30GM103519, P30GM110758]
We report remarkably high, up to 100-fold, signal enhancements in F-19 dynamic nuclear polarization (DNP) magic angle spinning (MAS) spectra at 14.1 T on HIV-1 capsid protein (CA) assemblies. These enhancements correspond to absolute sensitivity ratios of 12-29 and are of similar magnitude to those seen for H-1 signals in the same samples. At MAS frequencies above 20 kHz, it was possible to record 2D F-19-C-13 HETCOR spectra, which contain long-range intra- and intermolecular correlations. Such correlations provide unique distance restraints, inaccessible in conventional experiments without DNP, for protein structure determination. Furthermore, systematic quantification of the DNP enhancements as a function of biradical concentration, MAS frequency, temperature, and microwave power is reported. Our work establishes the power of DNP-enhanced F-19 MAS NMR spectroscopy for structural characterization of HIV-1 CA assemblies, and this approach is anticipated to be applicable to a wide range of large biomolecular systems.
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