메뉴 건너뛰기




Volumn 136, Issue 1, 1999, Pages 92-101

Sensitivity Improvement of Transverse Relaxation-Optimized Spectroscopy

Author keywords

Heteronuclear correlation; Macromolecules; NMR; Sensitivity improvement; TROSY

Indexed keywords

CALBINDIN; HYDROGEN; NERVE PROTEIN; PROTON;

EID: 0032622242     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.1998.1626     Document Type: Article
Times cited : (113)

References (33)
  • 1
    • 0030612833 scopus 로고    scopus 로고
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • 2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution, Proc. Natl. Acad. Sci. USA 94, 12366-12371 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 2
    • 48549112585 scopus 로고
    • Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei
    • M. Goldman, Interference effects in the relaxation of a pair of unlike spin-1/2 nuclei, J. Magn. Reson. 60, 437-452 (1984).
    • (1984) J. Magn. Reson. , vol.60 , pp. 437-452
    • Goldman, M.1
  • 3
    • 0000935329 scopus 로고
    • Theory of the dependence of nuclear magnetic relaxation on the absolute sign of spin-spin coupling constant
    • H. Shimizu, Theory of the dependence of nuclear magnetic relaxation on the absolute sign of spin-spin coupling constant, J. Chem. Phys. 40, 3357-3364 (1964).
    • (1964) J. Chem. Phys. , vol.40 , pp. 3357-3364
    • Shimizu, H.1
  • 4
    • 0020945346 scopus 로고
    • 15N-labeled nucleic acids via dipolar coupling and chemical shift anisotropy
    • 15N-labeled nucleic acids via dipolar coupling and chemical shift anisotropy, J. Am. Chem. Soc. 105, 7262-7266 (1983).
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 7262-7266
    • Guéron, M.1    Leroy, J.L.2    Griffey, R.H.3
  • 5
    • 0023284807 scopus 로고
    • Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution, Q
    • R. H. Griffey and A. G. Redfield, Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution, Q. Rev. Biophys. 19, 51-82 (1987).
    • (1987) Rev. Biophys. , vol.19 , pp. 51-82
    • Griffey, R.H.1    Redfield, A.G.2
  • 6
    • 44949289665 scopus 로고
    • Sensitivity improvement in isotropic mixing (TOCSY) experiments
    • J. Cavanagh and M. Rance, Sensitivity improvement in isotropic mixing (TOCSY) experiments, J. Magn. Reson. 88, 72-85 (1990).
    • (1990) J. Magn. Reson. , vol.88 , pp. 72-85
    • Cavanagh, J.1    Rance, M.2
  • 7
    • 0041381500 scopus 로고
    • Sensitivity improvement in multi-dimensional NMR spectroscopy
    • M. Rance, Sensitivity improvement in multi-dimensional NMR spectroscopy, Bull. Magn. Reson. 16, 54-67 (1994).
    • (1994) Bull. Magn. Reson. , vol.16 , pp. 54-67
    • Rance, M.1
  • 8
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy
    • A. G. Palmer, J. Cavanagh, P. E. Wright, and M. Rance, Sensitivity improvement in proton-detected two-dimensional heteronuclear correlation NMR spectroscopy, J. Magn. Reson. 93, 151-170 (1991).
    • (1991) J. Magn. Reson. , vol.93 , pp. 151-170
    • Palmer, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 9
    • 44049118891 scopus 로고
    • Sensitivity improvement in three-dimensional heteronuclear correlation NMR spectroscopy
    • A. G. Palmer, J. Cavanagh, R. A. Byrd, and M. Rance, Sensitivity improvement in three-dimensional heteronuclear correlation NMR spectroscopy, J. Magn. Reson. 96, 416-424 (1992).
    • (1992) J. Magn. Reson. , vol.96 , pp. 416-424
    • Palmer, A.G.1    Cavanagh, J.2    Byrd, R.A.3    Rance, M.4
  • 11
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • L. E. Kay, P. Keifer, and T. Saarinen, Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity, J. Am. Chem. Soc. 114, 10663-10665 (1992).
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 12
    • 0028472014 scopus 로고
    • Three-dimensional heteronuclear NMR spectroscopy with simultaneous isotope filtration, quadrature detection and sensitivity enhancement using z-rotation pulses
    • M. Akke, P. A. Carr, and A. G. Palmer, Three-dimensional heteronuclear NMR spectroscopy with simultaneous isotope filtration, quadrature detection and sensitivity enhancement using z-rotation pulses, J. Magn. Reson. B 104, 298-302 (1994).
    • (1994) J. Magn. Reson. B , vol.104 , pp. 298-302
    • Akke, M.1    Carr, P.A.2    Palmer, A.G.3
  • 15
    • 0000358511 scopus 로고
    • A simple formalism for the description of multiple-pulse experiments. Application to a weakly coupled two-spin (I = 1/2) system
    • F. J. M. van de Ven and C. W. Hilbers, A simple formalism for the description of multiple-pulse experiments. Application to a weakly coupled two-spin (I = 1/2) system, J. Magn. Reson. 54, 512-520 (1983).
    • (1983) J. Magn. Reson. , vol.54 , pp. 512-520
    • Van De Ven, F.J.M.1    Hilbers, C.W.2
  • 16
    • 0001674668 scopus 로고
    • The use of single-spin operator basis sets in the NMR spectroscopy of scalar-coupled spin systems
    • K. J. Packer and K. M. Wright, The use of single-spin operator basis sets in the NMR spectroscopy of scalar-coupled spin systems, Mol. Phys. 50, 797-813 (1983).
    • (1983) Mol. Phys. , vol.50 , pp. 797-813
    • Packer, K.J.1    Wright, K.M.2
  • 19
    • 0000486802 scopus 로고
    • Suppression of the effects of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms in the measurement of spin-spin relaxation rates
    • A. G. Palmer, N. J. Skelton, W. J. Chazin, P. E. Wright, and M. Rance, Suppression of the effects of cross-correlation between dipolar and anisotropic chemical shift relaxation mechanisms in the measurement of spin-spin relaxation rates, Mol. Phys. 75, 699-711 (1992).
    • (1992) Mol. Phys. , vol.75 , pp. 699-711
    • Palmer, A.G.1    Skelton, N.J.2    Chazin, W.J.3    Wright, P.E.4    Rance, M.5
  • 20
    • 84888390140 scopus 로고
    • Coherence transfer in the rotating frame. Application to heteronuclear cross-correlation spectroscopy
    • L. Müller and R. R. Ernst, Coherence transfer in the rotating frame. Application to heteronuclear cross-correlation spectroscopy, Mol. Phys. 38, 963-992 (1979).
    • (1979) Mol. Phys. , vol.38 , pp. 963-992
    • Müller, L.1    Ernst, R.R.2
  • 21
    • 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).
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 24
    • 0029338320 scopus 로고
    • Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation
    • S. Mori, C. Abeygunawardana, M. O'Neil Johnson, and P. C. M. van Zijl, Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation, J. Magn. Reson. B 108, 94-98 (1995).
    • (1995) J. Magn. Reson. B , vol.108 , pp. 94-98
    • Mori, S.1    Abeygunawardana, C.2    O'Neil Johnson, M.3    Van Zijl, P.C.M.4
  • 26
    • 0001909564 scopus 로고    scopus 로고
    • Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy
    • M. Liu, X.-a. Mao, C. Ye, H. Huang, J. K. Nicholson, and J. C. Lindon, Improved WATERGATE pulse sequences for solvent suppression in NMR spectroscopy, J. Magn. Reson. 132, 125-129 (1998).
    • (1998) J. Magn. Reson. , vol.132 , pp. 125-129
    • Liu, M.1    Mao, X.-A.2    Ye, C.3    Huang, H.4    Nicholson, J.K.5    Lindon, J.C.6
  • 27
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • M. Piotto, V. Saudek, and V. Sklenář, Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, J. Biomol. NMR 2, 661-665 (1992).
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenář, V.3
  • 28
    • 0000452256 scopus 로고
    • 1 baseline distortion and optimization of folding in multidimensional NMR spectra
    • 1 baseline distortion and optimization of folding in multidimensional NMR spectra, J. Magn. Reson. 91, 174-178 (1991).
    • (1991) J. Magn. Reson. , vol.91 , pp. 174-178
    • Bax, A.1    Ikura, M.2    Kay, L.E.3    Zhu, G.4
  • 30
  • 31
    • 0015394032 scopus 로고
    • Specificity and kinetics of triose phosphate isomerase from chicken muscle
    • S. J. Putman, A. F. Coulson, I. R. Farley, B. Riddleston, and J. R. Knowles, Specificity and kinetics of triose phosphate isomerase from chicken muscle, Biochem. J. 129, 301-310 (1972).
    • (1972) Biochem. J. , vol.129 , pp. 301-310
    • Putman, S.J.1    Coulson, A.F.2    Farley, I.R.3    Riddleston, B.4    Knowles, J.R.5
  • 32
    • 0029000872 scopus 로고
    • Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated
    • J. C. Williams and A. E. McDermott, Dynamics of the flexible loop of triosephosphate isomerase: The loop motion is not ligand gated, Biochemistry 34, 8309-8319 (1995).
    • (1995) Biochemistry , vol.34 , pp. 8309-8319
    • Williams, J.C.1    McDermott, A.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.