Details

Autor(en) / Beteiligte

• Jarvis, J. A
• Haies, I
• Lelli, M
• Rossini, A. J
• Kuprov, I
• Carravetta, M
• Williamson, P. T. F

Titel

Measurement of 14N quadrupole couplings in biomolecular solids using indirect-detection 14N solid-state NMR with DNPElectronic supplementary information (ESI) available: Detailed protocols for sample preparation and NMR data acquisition. Discussion on distribution of 14N shifts and resolution of sites in cryogenic DNP spectra. See DOI: 10.1039/c7cc03462h

Erscheinungsjahr

2017-11

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• The quadrupolar interaction experienced by the spin-1 14 N nucleus is known to be extremely sensitive to local structure and dynamics. Furthermore, the 14 N isotope is 99.6% naturally abundant, making it an attractive target for characterisation of nitrogen-rich biological molecules by solid-state NMR. In this study, dynamic nuclear polarization (DNP) is used in conjunction with indirect 14 N detected solid-state NMR experiments to simultaneously characterise the quadrupolar interaction at multiple 14 N sites in the backbone of the microcrystalline protein, GB3. Considerable variation in the quadrupolar interaction (>700 kHz) is observed throughout the protein backbone. The distribution in quadrupolar interactions observed reports on the variation in local backbone conformation and subtle differences in hydrogen-bonding; demonstrating a new route to the structural and dynamic analysis of biomolecules. Insights into protein structure through the determination of 14 N quadrupolar interactions using magic-angle spinning dynamic nuclear polarization NMR.