Browse > Article
http://dx.doi.org/10.5012/bkcs.2013.34.3.823

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)
Publication Information
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.
Keywords
Solid-state NMR probe; Low-${\varepsilon}$; Probe design; Membrane proteins; Bicelles;
Citations & Related Records
Times Cited By KSCI : 2  (Citation Analysis)
연도 인용수 순위
1 Nevzorov, A. A.; Opella, S. J. J. Magn. Reson. 2003, 164, 182.   DOI   ScienceOn
2 Martin, R. W.; Paulson, E. K.; Zilm, K. W. Rev. Sci. Instrum. 2003, 74, 3045.   DOI   ScienceOn
3 Wu, C. H.; Ramamoorthy, A.; Opella, S. J. J. Magn. Reson. A 1994, 109, 270.   DOI   ScienceOn
4 Nevzorov, A. A.; Opella, S. J. J. Magn. Reson. 2007, 185, 59.   DOI   ScienceOn
5 Wu, C. H.; Grant, C. V.; Cook, C. V.; Park, S. H.; Opella, S. J. J. Magn. Reson. 2009, 200, 74.   DOI   ScienceOn
6 Dvinskikh, S. V.; Castro, V.; Sandstrom, D. Magn. Reson. Chem. 2004, 42, 875.   DOI   ScienceOn
7 Li, C.; Mo, Y.; Hu, J.; Chekmenev, E. Y.; Tian, C.; Gao, F. P.; Fu, R.; Gor'kov, P. L.; Brey, W. W.; Cross, T. A. J. Magn. Reson. 2006, 180, 51.   DOI   ScienceOn
8 Gor'kov, P. L.; Chekmenev, E. Y.; Li, G. C.; Cotton, M.; Buffy, J. J.; Traaseth, N. J.; Veglia, G.; Brey, W. W. J. Magn. Reson. 2007, 185, 77.   DOI   ScienceOn
9 Grant, C. V.; Yang, Y.; Glibowicka, M.; Wu, C. H.; Park, S. H.; Deber, C. M.; Opella, S. J. J. Magn. Reson. 2009, 201, 87.   DOI   ScienceOn
10 Stringer, J. A.; Bronnimann, C. E.; Mullen, G. C.; Zhou, D. H.; Stellfox, S. A.; Li, Y.; Williams, E. H.; Rienstra, C. M. J. Magn. Reson. 2005, 173, 40.   DOI   ScienceOn
11 Wu, C. H.; Grant, C. V.; Cook, G. A.; Park, S. H.; Opella, S. J. J. Magn. Reson. 2009, 200, 74.   DOI   ScienceOn
12 Park, T. J.; Kim, J. S.; Um, S. H.; Kim, Y. Bull. Korean Chem. Soc. 2010, 31, 1187.   DOI   ScienceOn
13 Choi, S. S.; Jung, J. H.; Park, Y. G.; Park, T. J.; Park, G. H. J.; Kim, Y. Bull. Korean Chem. Soc. 2012, 33, 1577.   DOI   ScienceOn
14 Cross, V. R.; Hester, R. K.; Waugh, J. S. Rev. Sci. Instrum. 1976, 47, 1486.   DOI
15 Ammann, C.; Meier, P.; Merbach, A. J. Magn. Reson. 1982, 46, 319.
16 Pines, A.; Gibby, M. G.; Waugh, J. S. J. Chem. Phys. 1973, 59, 569.   DOI
17 Levitt, M. H. J. Chem. Phys. 1991, 94, 30.   DOI
18 Fung, B. M.; Khitrin, A. K.; Ermolaev, K. J. Magn. Reson. 2000, 142, 97.   DOI   ScienceOn
19 Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. J. Biomol. NMR 1995, 6, 277.
20 Sinha, N.; Grant, C. V.; Rotondi, K. S.; Feduik-Rotondi, L.; Gierasch, L. M.; Opella, S. J. J. Peptide Res. 2005, 65, 605.   DOI   ScienceOn