Low-ε Static Probe Development for 15 N- 1 H Solid-state NMR Study of Membrane Proteins for an 800 MHz NB Magnet

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...

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Veröffentlicht in:Bulletin of the Korean Chemical Society 2013, Vol.34 (3), p.823-826
Hauptverfasser: Park, Tae-Joon, Choi, Sung-Sub, Jung, Ji-Ho, Park, Yu-Geun, Kim, Yongae
Format: Artikel
Sprache:kor
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Zusammenfassung: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.
ISSN:0253-2964
1229-5949