期刊
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
卷 57, 期 50, 页码 16375-16379出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201809060
关键词
capsids; F-19 NMR spectroscopy; magic angle spinning; protein assemblies; protein structures
资金
- National Science Foundation (NSF) [CHE-1708773, CHE-0959496]
- National Institutes of Health (NIGMS)
- National Institutes of Health (NIAID) [P50 GM082251]
- National Institutes of Health (NIH) [P30GM103519, P30GM110758]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P50GM082251, P30GM103519, P30GM110758] Funding Source: NIH RePORTER
F-19 NMR spectroscopy is an attractive and growing area of research with broad applications in biochemistry, chemical biology, medicinal chemistry, and materials science. We have explored fast magic angle spinning (MAS) F-19 solid-state NMR spectroscopy in assemblies of HIV-1 capsid protein. Tryptophan residues with fluorine substitution at the 5-position of the indole ring were used as the reporters. The F-19 chemical shifts for the five tryptophan residues are distinct, reflecting differences in their local environment. Spin-diffusion and radio-frequency-driven-recoupling experiments were performed at MAS frequencies of 35 kHz and 40-60 kHz, respectively. Fast MAS frequencies of 40-60 kHz are essential for consistently establishing F-19-F-19 correlations, yielding interatomic distances of the order of 20 angstrom. Our results demonstrate the potential of fast MAS F-19 NMR spectroscopy for structural analysis in large biological assemblies.
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