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

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

Research output: Contribution to journalArticlepeer-review

Abstract

The quadrupolar interaction experienced by the spin-1 14N nucleus is known to be extremely sensitive to local structure and dynamics. Furthermore, the 14N 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 14N detected solid-state NMR experiments to simultaneously characterise the quadrupolar interaction at multiple 14N 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.

Original languageEnglish
Pages (from-to)12116-12119
Number of pages4
JournalChemical Communications
Volume53
Issue number89
DOIs
StatePublished - 2017
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • General Chemistry
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

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