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Volumn 45, Issue 3, 2009, Pages 311-318

Time-shared HSQC-NOESY for accurate distance constraints measured at high-field in 15N-13C-ILV methyl labeled proteins

Author keywords

Distance constraints; High resolution; NOESY; Non ribosomal peptide synthetases; Nuclear magnetic resonance; Protein structure; Time shared

Indexed keywords

CARBON 13; ISOLEUCINE; LEUCINE; NITROGEN 15; VALINE;

EID: 70350302655     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-009-9372-5     Document Type: Article
Times cited : (12)

References (35)
  • 1
    • 0003007299 scopus 로고
    • Exponential sampling, an alternative method for sampling in two-dimensional NMR experiments
    • Barna JCJ, Laue ED, Mayger MR, Skilling J, Worrall SJP (1987) Exponential sampling, an alternative method for sampling in two-dimensional NMR experiments. J Magn Reson 73:69-77
    • (1987) J Magn Reson , vol.73 , pp. 69-77
    • Barna, J.C.J.1    Laue, E.D.2    Mayger, M.R.3    Skilling, J.4    Worrall, S.J.P.5
  • 2
    • 0001669772 scopus 로고
    • Time-saving methods for heteronuclear multidimensional NMR of (13C, 15N) doubly labeled proteins
    • Boelens R, Burgering M, Fogh RH, Kaptein R (1994) Time-saving methods for heteronuclear multidimensional NMR of (13C, 15N) doubly labeled proteins. J Biomol NMR 4:201-213
    • (1994) J Biomol NMR , vol.4 , pp. 201-213
    • Boelens, R.1    Burgering, M.2    Fogh, R.H.3    Kaptein, R.4
  • 4
    • 0033612728 scopus 로고    scopus 로고
    • Relaxation of two-spin coherence due to cross-correlated fluctuations of dipole-dipole couplings and anisotropic shifts in NMR of 15N, 13C-labeled biomolecules
    • Chiarparin E, Pelupessy P, Ghose R, Bodenhausen G (1999) Relaxation of two-spin coherence due to cross-correlated fluctuations of dipole-dipole couplings and anisotropic shifts in NMR of 15N, 13C-labeled biomolecules. J Am Chem Soc 121:6876-6883
    • (1999) J Am Chem Soc , vol.121 , pp. 6876-6883
    • Chiarparin, E.1    Pelupessy, P.2    Ghose, R.3    Bodenhausen, G.4
  • 5
    • 0029400480 scopus 로고
    • NMRPipe a multidimensional spectra processing system based on UNIX pipes
    • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe a multidimensional spectra processing system based on UNIX pipes. JBNMR 6:277-293
    • (1995) JBNMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 6
    • 0000195125 scopus 로고
    • Simultaneous [13C, 15N]-HMQC, A pseudo-triple resonance experiment
    • Farmer B II (1991) Simultaneous [13C, 15N]-HMQC, A pseudo-triple resonance experiment. J Magn Reson 93:635-641
    • (1991) J Magn Reson , vol.93 , pp. 635-641
    • Farmer II, B.1
  • 7
    • 31444432912 scopus 로고    scopus 로고
    • Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment
    • Frueh DP, Arthanari H, Wagner G (2005) Unambiguous assignment of NMR protein backbone signals with a time-shared triple-resonance experiment. J Biomol NMR 33:187-196
    • (2005) J Biomol NMR , vol.33 , pp. 187-196
    • Frueh, D.P.1    Arthanari, H.2    Wagner, G.3
  • 8
    • 33644531581 scopus 로고    scopus 로고
    • Determination of all nOes in 1H-13C-Me-ILV-U-2H-15N proteins with two time-shared experiments
    • Frueh DP, Vosburg DA, Walsh CT, Wagner G (2006) Determination of all nOes in 1H-13C-Me-ILV-U-2H-15N proteins with two time-shared experiments. J Biomol NMR 34:31-40
    • (2006) J Biomol NMR , vol.34 , pp. 31-40
    • Frueh, D.P.1    Vosburg, D.A.2    Walsh, C.T.3    Wagner, G.4
  • 10
    • 0027787894 scopus 로고
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • 2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J Am Chem Soc 115:12593-12594
    • (1993) J Am Chem Soc , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 11
    • 57549109459 scopus 로고    scopus 로고
    • Identification of HN-methyl NOEs in large proteins using simultaneous amide-methyl TROSY-based detection
    • Guo C, Tugarinov V (2009) Identification of HN-methyl NOEs in large proteins using simultaneous amide-methyl TROSY-based detection. J Biomol NMR 43:21-30
    • (2009) J Biomol NMR , vol.43 , pp. 21-30
    • Guo, C.1    Tugarinov, V.2
  • 13
    • 70350303834 scopus 로고    scopus 로고
    • FM reconstruction of non-uniformly sampled protein NMR data at higher dimensions and optimization by distillation
    • doi: 10.1007/s10858-009-9368-1
    • Hyberts S, Frueh D, Arthanari H, Wagner G (2009) FM reconstruction of non-uniformly sampled protein NMR data at higher dimensions and optimization by distillation. J Biomol NMR. doi: 10.1007/ s10858-009-9368-1
    • (2009) J Biomol NMR
    • Hyberts, S.1    Frueh, D.2    Arthanari, H.3    Wagner, G.4
  • 14
    • 0002551301 scopus 로고
    • A 3D 1H, 15N and 13C NOESY correlating experiment
    • Jerala R, Rule G (1995) A 3D 1H, 15N and 13C NOESY correlating experiment. J Magn Reson 108:294-298
    • (1995) J Magn Reson , vol.108 , pp. 294-298
    • Jerala, R.1    Rule, G.2
  • 17
    • 0042386728 scopus 로고    scopus 로고
    • A combined HNCA/HNCO experiment for 15N labeled proteins with 13C at natural abundance
    • Kupce E, Muhandiram DR, Kay LE (2003) A combined HNCA/HNCO experiment for 15N labeled proteins with 13C at natural abundance. J Biomol NMR 27:175-179
    • (2003) J Biomol NMR , vol.27 , pp. 175-179
    • Kupce, E.1    Muhandiram, D.R.2    Kay, L.E.3
  • 18
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • Marion D, Ikura M, Tschudin R, Bax A (1989) Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. JMR 85:393-399
    • (1989) JMR , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4
  • 19
    • 0033210868 scopus 로고    scopus 로고
    • Suppression of diagonal peaks in TROSY-type 1H NMR NOESY spectra of 15N-labeled proteins
    • Meissner A, Sorensen OW (1999) Suppression of diagonal peaks in TROSY-type 1H NMR NOESY spectra of 15N-labeled proteins. J Magn Reson 140:499-503
    • (1999) J Magn Reson , vol.140 , pp. 499-503
    • Meissner, A.1    Sorensen, O.W.2
  • 20
    • 0034981892 scopus 로고    scopus 로고
    • MUNIN: A new approach to multi-dimensional NMR spectra interpretation
    • Orekhov VY, Ibraghimov IV, Billeter M (2001) MUNIN: A new approach to multi-dimensional NMR spectra interpretation. J Biomol NMR 20:49-60
    • (2001) J Biomol NMR , vol.20 , pp. 49-60
    • Orekhov, V.Y.1    Ibraghimov, I.V.2    Billeter, M.3
  • 23
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenar V (1992) Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 2:661-665
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 24
    • 4243138246 scopus 로고    scopus 로고
    • Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction
    • Rovnyak D, Frueh DP, Sastry M, Sun ZY, Stern AS, Hoch JC, Wagner G (2004) Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction. J Magn Reson 170:15-21
    • (2004) J Magn Reson , vol.170 , pp. 15-21
    • Rovnyak, D.1    Frueh, D.P.2    Sastry, M.3    Sun, Z.Y.4    Stern, A.S.5    Hoch, J.C.6    Wagner, G.7
  • 25
    • 0002522872 scopus 로고
    • A simultaneous 15N.1H and 13C, 1H-HSQC with sensitivity enhancement and a heteronuclear gradient echo
    • Sattler M, Maurer M, Schleucher J, Griesinger C (1995) A simultaneous 15N.1H and 13C, 1H-HSQC with sensitivity enhancement and a heteronuclear gradient echo. J Biomol NMR 5:97-102
    • (1995) J Biomol NMR , vol.5 , pp. 97-102
    • Sattler, M.1    Maurer, M.2    Schleucher, J.3    Griesinger, C.4
  • 26
    • 0027661526 scopus 로고
    • Application of nonlinear sampling schemes to COSY-type spectra
    • Schmieder P, Stern AS, Wagner G, Hoch JC (1993) Application of nonlinear sampling schemes to COSY-type spectra. J Biomol NMR 3:569-576
    • (1993) J Biomol NMR , vol.3 , pp. 569-576
    • Schmieder, P.1    Stern, A.S.2    Wagner, G.3    Hoch, J.C.4
  • 27
    • 13444269041 scopus 로고
    • Computer-optimized decoupling scheme for wideband applications and low-level operation
    • Shaka AJ, Barker P, 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.2    Freeman, R.3
  • 28
    • 48749147783 scopus 로고
    • An improved sequence for broadband decoupling: WALTZ-16
    • Shaka AJ, Keeler J, Frenkiel T, Freeman R (1983) An improved sequence for broadband decoupling: WALTZ-16. J Magn Reson 52:335-338
    • (1983) J Magn Reson , vol.52 , pp. 335-338
    • Shaka, A.J.1    Keeler, J.2    Frenkiel, T.3    Freeman, R.4
  • 29
    • 0002458951 scopus 로고
    • Aspects and prospects of multidimensional time-domain spectroscopy
    • 1969
    • Sørensen O (1990) Aspects and prospects of multidimensional time-domain spectroscopy. J Magn Reson 89:210-216 1969
    • (1990) J Magn Reson , vol.89 , pp. 210-216
    • Sørensen, O.1
  • 30
    • 0030207171 scopus 로고    scopus 로고
    • An optimized 3D NOESY-HSQC
    • Talluri S, Wagner G (1996) An optimized 3D NOESY-HSQC. J Magn Reson B 112:200-205
    • (1996) J Magn Reson B , vol.112 , pp. 200-205
    • Talluri, S.1    Wagner, G.2
  • 31
    • 14744278812 scopus 로고    scopus 로고
    • High-resolution four-dimensional 1H-13C NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition
    • Tugarinov V, Kay LE, Ibraghimov I, Orekhov VY (2005) High-resolution four-dimensional 1H-13C NOE spectroscopy using methyl-TROSY, sparse data acquisition, and multidimensional decomposition. J Am Chem Soc 127:2767-2775
    • (2005) J Am Chem Soc , vol.127 , pp. 2767-2775
    • Tugarinov, V.1    Kay, L.E.2    Ibraghimov, I.3    Orekhov, V.Y.4
  • 32
    • 0033622497 scopus 로고    scopus 로고
    • Simultaneous CT-13C and VT-15N chemical shift labelling: Application to 3D NOESY-CH3NH and 3D 13C, 15N HSQC-NOESY-CH3NH
    • Uhrín D, Bramham J, Winder SJ, Barlow PN (2000) Simultaneous CT-13C and VT-15N chemical shift labelling: Application to 3D NOESY-CH3NH and 3D 13C, 15N HSQC-NOESY-CH3NH. J Biomol NMR 18:253-259
    • (2000) J Biomol NMR , vol.18 , pp. 253-259
    • Uhrín, D.1    Bramham, J.2    Winder, S.J.3    Barlow, P.N.4
  • 33
    • 34548495116 scopus 로고    scopus 로고
    • Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: Application to binding epitope mapping
    • Wurtz P, Aitio O, Hellman M, Permi P (2007) Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping. J Biomol NMR 39:97-105
    • (2007) J Biomol NMR , vol.39 , pp. 97-105
    • Wurtz, P.1    Aitio, O.2    Hellman, M.3    Permi, P.4
  • 34
    • 0035040149 scopus 로고    scopus 로고
    • 3D Haro-NOESY-CH3NH and Caro-NOESY-CH3NH experiments for double labeled proteins
    • Xia Y, Zhu G (2001) 3D Haro-NOESY-CH3NH and Caro-NOESY-CH3NH experiments for double labeled proteins. J Biomol NMR 19:355-360
    • (2001) J Biomol NMR , vol.19 , pp. 355-360
    • Xia, Y.1    Zhu, G.2
  • 35
    • 0032885432 scopus 로고    scopus 로고
    • 2D and 3D TROSY-enhanced NOESY of 15N labeled proteins
    • Zhu G, Xia Y, Sze KH, Yan X (1999) 2D and 3D TROSY-enhanced NOESY of 15N labeled proteins. J Biomol NMR 14:377-381
    • (1999) J Biomol NMR , vol.14 , pp. 377-381
    • Zhu, G.1    Xia, Y.2    Sze, K.H.3    Yan, X.4


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