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Volumn 44, Issue 2, 2009, Pages 69-76

The T-lock: Automated compensation of radio-frequency induced sample heating

Author keywords

Calibration; Chemical shifts; NMR; Temperature control

Indexed keywords

ALANINE; ARGININE; CARBON 13; OXYGEN 17; PHOSPHATE; PHOSPHORUS 31; WATER;

EID: 67349248429     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9319-x     Document Type: Article
Times cited : (6)

References (34)
  • 1
    • 0001217756 scopus 로고
    • A simple multinuclear NMR thermometer
    • Ammann C, Meier P, Merbach AE (1982) A simple multinuclear NMR thermometer. J Magn Reson 46:319-321
    • (1982) J Magn Reson , vol.46 , pp. 319-321
    • Ammann, C.1    Meier, P.2    Merbach, A.E.3
  • 5
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing - Application to proton correlation spectroscopy
    • Braunschweiler L, Ernst RR (1983) Coherence transfer by isotropic mixing - application to proton correlation spectroscopy. J Magn Reson 53:521-528
    • (1983) J Magn Reson , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 7
    • 0018934355 scopus 로고
    • Chemical shift thermometer for phosphorous-31 nuclear magnetic resonance measurements
    • Dickert FL, Hellmann SW (1980) Chemical shift thermometer for phosphorous-31 nuclear magnetic resonance measurements. Anal Chem 52:996-998
    • (1980) Anal Chem , vol.52 , pp. 996-998
    • Dickert, F.L.1    Hellmann, S.W.2
  • 8
    • 0000568960 scopus 로고
    • An inexpensive precise gas flow temperature controller
    • Farrar TC, Sidky E, Decatur JD (1990) An inexpensive precise gas flow temperature controller. J Magn Reson 86:605-612
    • (1990) J Magn Reson , vol.86 , pp. 605-612
    • Farrar, T.C.1    Sidky, E.2    Decatur, J.D.3
  • 11
    • 3242798849 scopus 로고    scopus 로고
    • A simple method for improving protein solubility and long-term stability
    • Golovanov AP, Hautbergue GM, Wilson SA, Lian LY (2004) A simple method for improving protein solubility and long-term stability. J Am Chem Soc 126:8933-8939
    • (2004) J Am Chem Soc , vol.126 , pp. 8933-8939
    • Golovanov, A.P.1    Hautbergue, G.M.2    Wilson, S.A.3    Lian, L.Y.4
  • 13
    • 0031714689 scopus 로고    scopus 로고
    • Structure calculation of biological macromolecules from NMR data
    • Güntert P (1998) Structure calculation of biological macromolecules from NMR data. Q Rev Biophys 31:145-237
    • (1998) Q Rev Biophys , vol.31 , pp. 145-237
    • Güntert, P.1
  • 14
    • 0020484560 scopus 로고
    • 6A-U from proton NMR chemical shifts: Differential concentration temperature profile method
    • 6A-U from proton NMR chemical shifts: Differential concentration temperature profile method. Eur J Biochem 129:343-357
    • (1982) Eur J Biochem , vol.129 , pp. 343-357
    • Hartel, A.J.1    Lankhorst, P.P.2    Altona, C.3
  • 15
    • 0000871046 scopus 로고    scopus 로고
    • 1H NMR and suppression of convection in NMR probes
    • 1H NMR and suppression of convection in NMR probes. J Magn Reson 131:126-130
    • (1998) J Magn Reson , vol.131 , pp. 126-130
    • Hedin, N.1    Furo, I.I.2
  • 16
    • 55649094172 scopus 로고    scopus 로고
    • APSY-NMR with proteins: Practical aspects and backbone assignment
    • Hiller S. Wider G. Wüthrich K. 2008 APSY-NMR with proteins: Practical aspects and backbone assignment. J Biomol NMR 42 179-195
    • (2008) J Biomol NMR , vol.42 , pp. 179-195
    • Hiller, S.1    Wider, G.2    Wüthrich, K.3
  • 18
    • 0000468681 scopus 로고    scopus 로고
    • Thermal convection currents in NMR: Flow profiles and implications for coherence pathway selection
    • Jerschow A (2000) Thermal convection currents in NMR: Flow profiles and implications for coherence pathway selection. J Magn Reson 145:125-131
    • (2000) J Magn Reson , vol.145 , pp. 125-131
    • Jerschow, A.1
  • 19
    • 0017980508 scopus 로고
    • Automatic NMR field-frequency lock-pulsed phase locked loop approach
    • Kan S, Gonord P, Fan M, Sauzade M, Courtieu J (1978) Automatic NMR field-frequency lock-pulsed phase locked loop approach. Rev Sci Instrum 49:785-789
    • (1978) Rev Sci Instrum , vol.49 , pp. 785-789
    • Kan, S.1    Gonord, P.2    Fan, M.3    Sauzade, M.4    Courtieu, J.5
  • 20
    • 67349242399 scopus 로고
    • Patent application 3-156394, Japan
    • Keiichiro H (1991) Patent application 3-156394, Japan
    • (1991)
    • Keiichiro, H.1
  • 21
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE)-experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A, Ernst RR, Wüthrich K (1980) A two-dimensional nuclear Overhauser enhancement (2D NOE)-experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem Biophys Res Commun 95:1-6
    • (1980) Biochem Biophys Res Commun , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wüthrich, K.3
  • 22
    • 0000985728 scopus 로고
    • A sensitive NMR thermometer for multinuclei FT NMR
    • Levy GC, Bailey FT, Wright DA (1980) A sensitive NMR thermometer for multinuclei FT NMR. J Magn Reson 37:353-356
    • (1980) J Magn Reson , vol.37 , pp. 353-356
    • Levy, G.C.1    Bailey, F.T.2    Wright, D.A.3
  • 23
    • 84890928276 scopus 로고
    • An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically enriched proteins
    • Montelione GT, Lyons BA, Emerson SD, Tashiro M (1992) An efficient triple resonance experiment using carbon-13 isotropic mixing for determining sequence-specific resonance assignments of isotopically enriched proteins. J Am Chem Soc 114:10974-10975
    • (1992) J Am Chem Soc , vol.114 , pp. 10974-10975
    • Montelione, G.T.1    Lyons, B.A.2    Emerson, S.D.3    Tashiro, M.4
  • 24
    • 0014688629 scopus 로고
    • Temperature dependence of amide proton chemical shifts - Secondary structures of gramicidin S and valinomycin
    • Ohnishi M, Urry DW (1969) Temperature dependence of amide proton chemical shifts - secondary structures of gramicidin S and valinomycin. Biochem Biophys Res Commun 36:194-202
    • (1969) Biochem Biophys Res Commun , vol.36 , pp. 194-202
    • Ohnishi, M.1    Urry, D.W.2
  • 25
    • 0000721278 scopus 로고    scopus 로고
    • A high-precision carbon-13 shift thermometer for the temperature range 100-300 K
    • Quast H, Heubes M, Dunger A, Limbach HH (1998) A high-precision carbon-13 shift thermometer for the temperature range 100-300 K. J Magn Reson 134:236-244
    • (1998) J Magn Reson , vol.134 , pp. 236-244
    • Quast, H.1    Heubes, M.2    Dunger, A.3    Limbach, H.H.4
  • 26
    • 33645898633 scopus 로고    scopus 로고
    • Determination of sample temperature and temperature stability with 129 Xe NMR
    • Saunavaara J, Jokisaari J (2006) Determination of sample temperature and temperature stability with 129 Xe NMR. J Magn Reson 180:58-62
    • (2006) J Magn Reson , vol.180 , pp. 58-62
    • Saunavaara, J.1    Jokisaari, J.2
  • 27
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka AJ, Barker PB, Freeman R (1985) Computer-optimized decoupling scheme for wideband applications and low-level operation. J Magn Reson 64:547-552
    • (1985) J Magn Reson , vol.64 , pp. 547-552
    • Shaka, A.J.1    Barker, P.B.2    Freeman, R.3
  • 29
    • 33947294445 scopus 로고
    • Calibration of methanol nuclear magnetic resonance thermometer at low temperature
    • van Geet AL (1970) Calibration of methanol nuclear magnetic resonance thermometer at low temperature. Anal Chem 42:679-680
    • (1970) Anal Chem , vol.42 , pp. 679-680
    • van Geet, A.L.1
  • 30
    • 0027690573 scopus 로고
    • Minimizing the effects of radio-frequency heating in multidimensional NMR experiments
    • Wang AC, Bax A (1993) Minimizing the effects of radio-frequency heating in multidimensional NMR experiments. J Biomol NMR 3:715-720
    • (1993) J Biomol NMR , vol.3 , pp. 715-720
    • Wang, A.C.1    Bax, A.2
  • 31
    • 0000961515 scopus 로고    scopus 로고
    • Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution
    • Wider G (1998) Technical aspects of NMR spectroscopy with biological macromolecules and studies of hydration in solution. Prog Nucl Magn Reson Spectrosc 32:193-275
    • (1998) Prog Nucl Magn Reson Spectrosc , vol.32 , pp. 193-275
    • Wider, G.1
  • 32
    • 34447561861 scopus 로고    scopus 로고
    • Real-time imaging of the spatial distribution of rf-heating in NMR samples during broadband decoupling
    • Wimmer R, Wider G (2007) Real-time imaging of the spatial distribution of rf-heating in NMR samples during broadband decoupling. J Magn Reson 187:184-192
    • (2007) J Magn Reson , vol.187 , pp. 184-192
    • Wimmer, R.1    Wider, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.