Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Low-ε Static Probe Development for 15N-1H Solid-state NMR Study of Membrane Proteins for an 800 MHz NB Magnet

  • Park, Tae-Joon (Department of Chemistry and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies) ;
  • Choi, Sung-Sub (Department of Chemistry and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies) ;
  • Jung, Ji-Ho (Department of Chemistry and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies) ;
  • Park, Yu-Geun (Department of Chemistry and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies) ;
  • Kim, Yongae (Department of Chemistry and Protein Research Center for Bio-Industry, Hankuk University of Foreign Studies)
  • Received : 2012.11.05
  • Accepted : 2012.12.12
  • Published : 2013.03.20
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Abstract

A low-${\varepsilon}$ solid-state NMR(Nuclear Magnetic Resonance) probe was developed for the spectroscopic analysis of two-dimensional $^{15}N-^1H$ heteronuclear dipolar coupling in dilute membrane proteins oriented in hydrated and dielectrically lossy lipid environments. The system employed a 800 MHz narrow-bore magnet. A solenoid coil strip shield was used to reduce deleterious RF sample heating by minimizing the conservative electric fields generated by the double-tuned resonator at high magnetic fields. The probe's design, construction, and performance in solid-state NMR experiments at high magnetic fields are described here. Such high-resolution solid-state NMR spectroscopic analysis of static oriented samples in hydrated phospholipid bilayers or bicelles could aid the structural analysis of dilute biological membrane proteins.

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References

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