Reduction of RF-induced sample heating with a scroll coil resonator structure for solid-state NMR probes

John A. Stringer, Charles E. Bronnimann, Charles G. Mullen, Donghua H. Zhou, Sara A. Stellfox, Ying Li, Evan H. Williams, Chad M. Rienstra

Research output: Contribution to journalArticlepeer-review


Heating due to high power 1H decoupling limits the experimental lifetime of protein samples for solid-state NMR (SSNMR). Sample deterioration can be minimized by lowering the experimental salt concentration, temperature or decoupling fields; however, these approaches may compromise biological relevance and/or spectroscopic resolution and sensitivity. The desire to apply sophisticated multiple pulse experiments to proteins therefore motivates the development of probes that utilize the RF power more efficiently to generate a high ratio of magnetic to electric field in the sample. Here a novel scroll coil resonator structure is presented and compared to a traditional solenoid. The scroll coil is demonstrated to be more tolerant of high sample salt concentrations and cause less RF-induced sample heating. With it, the viable experimental lifetime of a microcrystalline ubiquitin sample has been extended by more than an order of magnitude. The higher B1 homogeneity and permissible decoupling fields enhance polarization transfer efficiency in 15N-13C correlation experiments employed for protein chemical shift assignments and structure determination.

Original languageEnglish (US)
Pages (from-to)40-48
Number of pages9
JournalJournal of Magnetic Resonance
Issue number1
StatePublished - Mar 2005


  • Dielectric
  • Heating
  • Probe
  • Protein
  • Salt
  • Scroll
  • Solenoid
  • Solid-state NMR spectroscopy

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Nuclear and High Energy Physics
  • Condensed Matter Physics

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