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Volumn 171, Issue 2, 2004, Pages 338-344

The set of triple-resonance sequences with a multiple quantum coherence evolution period

Author keywords

Coupling constants; H(N)COCA; HN(CO)CA; HNCA; HNCO; HNCOCA; Multiple quantum evolution; Reduced dimensionality; Sequential assignment; Triple resonance; Ubiquitin

Indexed keywords

COHERENT LIGHT; DATA ACQUISITION; NATURAL FREQUENCIES; PH EFFECTS; PHASE MODULATION; RESONANCE; SIGNAL TO NOISE RATIO;

EID: 9544258267     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmr.2004.09.013     Document Type: Article
Times cited : (3)

References (34)
  • 2
    • 0006393051 scopus 로고
    • Two-dimensional spectros-copy. Application to nuclear magnetic resonance
    • W.P. Aue, E. Bartholdi, R.R. Ernst, Two-dimensional spectros-copy. Application to nuclear magnetic resonance, J. Chem. Phys. 64 (1976) 2229-2246.
    • (1976) J. Chem. Phys. , vol.64 , pp. 2229-2246
    • Aue, W.P.1    Bartholdi, E.2    Ernst, R.R.3
  • 3
    • 18744411499 scopus 로고    scopus 로고
    • The acquisition of multidimensional NMR spectra within a single scan
    • L. Frydman, T. Scherf, A. Lupulescu, The acquisition of multidimensional NMR spectra within a single scan, Proc. Natl. Acad. Sci. USA 99 (2002) 15662-15858.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15662-15858
    • Frydman, L.1    Scherf, T.2    Lupulescu, A.3
  • 4
    • 0042868578 scopus 로고    scopus 로고
    • Principles and features of single-scan two-dimensional NMR spectroscopy
    • L. Frydman, A. Lupulescu, T. Scherf, Principles and features of single-scan two-dimensional NMR spectroscopy, J. Am. Chem. Soc. 125 (2003) 9204-9217.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9204-9217
    • Frydman, L.1    Lupulescu, A.2    Scherf, T.3
  • 5
    • 0042693083 scopus 로고    scopus 로고
    • Single-scan NMR spectroscopy at arbitrary dimensions
    • Y. Shrot, L. Frydman, Single-Scan NMR spectroscopy at arbitrary dimensions, J. Am. Chem. Soc. 125(2003) 11385-11396.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11385-11396
    • Shrot, Y.1    Frydman, L.2
  • 6
    • 0141957548 scopus 로고    scopus 로고
    • Adiabatic single scan two-dimensional NMR spectrocopy
    • P. Pelupessy, Adiabatic single scan two-dimensional NMR spectrocopy, J. Am. Chem. Soc. 125 (2003) 12345-12350.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 12345-12350
    • Pelupessy, P.1
  • 7
    • 0041886427 scopus 로고    scopus 로고
    • New methods for fast multidimensional NMR
    • Ē. Kupče, R. Freeman, New methods for fast multidimensional NMR, J. Biomol. NMR 27 (2003) 101-113.
    • (2003) J. Biomol. NMR , vol.27 , pp. 101-113
    • Kupče, E.1    Freeman, R.2
  • 8
    • 0041399068 scopus 로고    scopus 로고
    • Reconstruction of the three-dimensional NMR spectrum of a protein from a set of plane projections
    • Ē. Kupče, R. Freeman, Reconstruction of the three-dimensional NMR spectrum of a protein from a set of plane projections, J. Biomol. NMR 27 (2003) 383-387.
    • (2003) J. Biomol. NMR , vol.27 , pp. 383-387
    • Kupče, E.1    Freeman, R.2
  • 9
    • 0242498378 scopus 로고    scopus 로고
    • Projection-reconstruction of three-dimensional NMR spectra
    • Ē. Kupče, R. Freeman, Projection-reconstruction of three-dimensional NMR spectra, J. Am. Chem. Soc. 125 (2003) 13958-13959.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13958-13959
    • Kupče, E.1    Freeman, R.2
  • 10
    • 0942265482 scopus 로고    scopus 로고
    • Generalized reconstruction of n-D NMR spectra from multiple projections: Application to the 5-D HACACONH spectrum of protein G B1 domain
    • B.E. Coggins, R.A. Venters, P. Zhou, Generalized reconstruction of n-D NMR spectra from multiple projections: application to the 5-D HACACONH spectrum of protein G B1 domain, J. Am. Chem. Soc. 126 (2004) 1000-1001.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1000-1001
    • Coggins, B.E.1    Venters, R.A.2    Zhou, P.3
  • 12
    • 0002930297 scopus 로고
    • Design of a complete set of two-dimensional triple-resonance experiments for assigning labeled proteins
    • B. Brutscher, J.P. Simorre, M.S. Caffrey, D. Marion, Design of a complete set of two-dimensional triple-resonance experiments for assigning labeled proteins, J. Magn. Reson. B 105 (1994) 77-82.
    • (1994) J. Magn. Reson. B , vol.105 , pp. 77-82
    • Brutscher, B.1    Simorre, J.P.2    Caffrey, M.S.3    Marion, D.4
  • 13
    • 0001436130 scopus 로고
    • A new triple-resonance experiment for the sequential assignment of backbone resonances in proteins
    • F. Löhr, H. Rüterjans, A new triple-resonance experiment for the sequential assignment of backbone resonances in proteins, J. Biomol. NMR 6 (1995) 189-197.
    • (1995) J. Biomol. NMR , vol.6 , pp. 189-197
    • Löhr, F.1    Rüterjans, H.2
  • 14
    • 0036041999 scopus 로고    scopus 로고
    • Novel 2D triple-resonance NMR experiments for sequential resonance assignments of proteins
    • K. Ding, A.M. Gronenborn, Novel 2D triple-resonance NMR experiments for sequential resonance assignments of proteins, J. Magn. Reson. 156 (2002) 262-268.
    • (2002) J. Magn. Reson. , vol.156 , pp. 262-268
    • Ding, K.1    Gronenborn, A.M.2
  • 15
    • 0042526130 scopus 로고    scopus 로고
    • Optimized set of two-dimensional experiments for fast sequential assignment, secondary structure determination, and backbone fold validation of 13C/ 15N-labelled proteins
    • B. Bersch, E. Rossy, J. Coves, B. Bratscher, Optimized set of two-dimensional experiments for fast sequential assignment, secondary structure determination, and backbone fold validation of 13C/ 15N-labelled proteins, J. Biomol. NMR 27 (2003) 57-67.
    • (2003) J. Biomol. NMR , vol.27 , pp. 57-67
    • Bersch, B.1    Rossy, E.2    Coves, J.3    Bratscher, B.4
  • 16
    • 0037986808 scopus 로고    scopus 로고
    • Multiple quadrature detection in reduced dimensionality experiments
    • W. Koźmiński, J. Zhukov, Multiple quadrature detection in reduced dimensionality experiments, J. Biomol. NMR 26 (2003) 157-166.
    • (2003) J. Biomol. NMR , vol.26 , pp. 157-166
    • Koźmiński, W.1    Zhukov, J.2
  • 17
    • 0037419802 scopus 로고    scopus 로고
    • GFT NMR, a new approach to rapidly obtain precise high-dimensional NMR spectral information
    • S. Kim, T. Szyperski, GFT NMR, a new approach to rapidly obtain precise high-dimensional NMR spectral information, J. Am. Chem. Soc. 125 (2003) 1385-1393.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1385-1393
    • Kim, S.1    Szyperski, T.2
  • 18
    • 49049148770 scopus 로고
    • The accordion experiment, a simple approach to three-dimensional NMR spectroscopy
    • G. Bodenhausen, R.R. Ernst, The accordion experiment, a simple approach to three-dimensional NMR spectroscopy, J. Magn. Reson. 45 (1981) 367-373.
    • (1981) J. Magn. Reson. , vol.45 , pp. 367-373
    • Bodenhausen, G.1    Ernst, R.R.2
  • 19
    • 0020102878 scopus 로고
    • Direct determination of rate constants of slow dynamic processes by two-dimensional accordion spectroscopy in nuclear magnetic resonance
    • G. Bodenhausen, R.R. Ernst, Direct determination of rate constants of slow dynamic processes by two-dimensional accordion spectroscopy in nuclear magnetic resonance, J. Am. Chem. Soc. 104 (1982) 1304-1309.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1304-1309
    • Bodenhausen, G.1    Ernst, R.R.2
  • 20
    • 1242331367 scopus 로고    scopus 로고
    • Triple resonance MAS NMR with (13C, 15N) labelled molecules: Reduced dimensionality data acquisition Via 13C-15N heteronuclear two-spin coherence transfer pathways
    • J. Leppert, B. Heise, O. Ohlenschläger, M. Görlach, R. Ramachandran, Triple resonance MAS NMR with (13C, 15N) labelled molecules: reduced dimensionality data acquisition Via 13C-15N heteronuclear two-spin coherence transfer pathways, J. Biomol. NMR 28 (2004) 185-190.
    • (2004) J. Biomol. NMR , vol.28 , pp. 185-190
    • Leppert, J.1    Heise, B.2    Ohlenschläger, O.3    Görlach, M.4    Ramachandran, R.5
  • 21
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
    • A.G. Palmer III, J. Cavanagh, P.E. Wright, M. Rance, Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy, J. Magn. Reson. 93 (1991) 151-170.
    • (1991) J. Magn. Reson. , vol.93 , pp. 151-170
    • Palmer III, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 22
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • L.E. Kay, P. Keifer, T. Saarinen, Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity, J. Am. Chem. Soc. 114 (1992) 10663-10665.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 23
    • 34249757083 scopus 로고
    • Novel strategies for sensitivity enhancement in heteronuclear multidimensional NMR experiments employing pulsed firl gradients
    • M. Sattler, M.G. Schwedinger, J. Schleuchter, C. Griesinger, Novel strategies for sensitivity enhancement in heteronuclear multidimensional NMR experiments employing pulsed firl gradients, J. Biomol. NMR 5 (1995) 11-22.
    • (1995) J. Biomol. NMR , vol.5 , pp. 11-22
    • Sattler, M.1    Schwedinger, M.G.2    Schleuchter, J.3    Griesinger, C.4
  • 24
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • M. Sattler, J. Schleuchter, C. Griesinger, Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients, Prog. NMR Spectrosc. 34 (1999) 93-158.
    • (1999) Prog. NMR Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleuchter, J.2    Griesinger, C.3
  • 26
    • 0021114895 scopus 로고
    • Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins
    • D. Marion, K. Wüthrich, Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins, Biochem. Biophys. Res. Commun. 113 (1983) 967-974.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 967-974
    • Marion, D.1    Wüthrich, K.2
  • 27
    • 0033599567 scopus 로고    scopus 로고
    • TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein
    • D. Yang, L.E. Kay, TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein, J. Am. Chem. Soc. 121 (1999) 2571-2575.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2571-2575
    • Yang, D.1    Kay, L.E.2
  • 29
    • 0001697580 scopus 로고
    • New principle for the determination of coupling constants that largely suppresses differential relaxation effects
    • A. Rexroth, P. Schimdt, S. Szalma, T. Geppert, H. Schwalbe, C. Griesinger, New principle for the determination of coupling constants that largely suppresses differential relaxation effects, J. Am. Chem. Soc. 117 (1995) 10389-10390.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10389-10390
    • Rexroth, A.1    Schimdt, P.2    Szalma, S.3    Geppert, T.4    Schwalbe, H.5    Griesinger, C.6
  • 31
    • 0037215324 scopus 로고    scopus 로고
    • Weak alignment offers new NMR opportunities to study protein structure and dynamics
    • A. Bax, Weak alignment offers new NMR opportunities to study protein structure and dynamics, Protein Sci. 12 (2003) 1-16.
    • (2003) Protein Sci. , vol.12 , pp. 1-16
    • Bax, A.1
  • 32
    • 0000968918 scopus 로고
    • Composite pulses for ultra-broadband spin inversion
    • A.J. Shaka, Composite pulses for ultra-broadband spin inversion, Chem. Phys. Lett. 120 (1985) 201-205.
    • (1985) Chem. Phys. Lett. , vol.120 , pp. 201-205
    • Shaka, A.J.1
  • 33
    • 2642628181 scopus 로고
    • Two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants
    • D.J. States, R.A. Haberkorn, R.J. Ruben, Two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants, J. Magn. Reson. 48 (1982) 286-292.
    • (1982) J. Magn. Reson. , vol.48 , pp. 286-292
    • States, D.J.1    Haberkorn, R.A.2    Ruben, R.J.3
  • 34
    • 45249127991 scopus 로고
    • Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins
    • D. Marion, M. Ikura, R. Tschudin, A. Bax, Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins, J. Magn. Reson. 85 (1989) 393-399.
    • (1989) J. Magn. Reson. , vol.85 , pp. 393-399
    • Marion, D.1    Ikura, M.2    Tschudin, R.3    Bax, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.