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Default Measurement of (14)N quadrupole couplings in biomolecular solids using indirect-detection (14)N solid-state NMR with DNP.

Measurement of (14)N quadrupole couplings in biomolecular solids using indirect-detection (14)N solid-state NMR with DNP.

Related Articles Measurement of (14)N quadrupole couplings in biomolecular solids using indirect-detection (14)N solid-state NMR with DNP.

Chem Commun (Camb). 2017 Oct 26;:

Authors: Jarvis JA, Haies I, Lelli M, Rossini AJ, Kuprov I, Carravetta M, Williamson PTF

Abstract
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.


PMID: 29072716 [PubMed - as supplied by publisher]



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