메뉴 건너뛰기




Volumn 163, Issue 1, 2003, Pages 92-98

JE-TROSY: Combined J- and TROSY-spectroscopy for the measurement of one-bond couplings in macromolecules

Author keywords

J spectroscopy; Protein; Residual dipolar couplings; RNA; Scalar couplings; TROSY

Indexed keywords

COMPLEXATION; CROSSTALK; FREQUENCIES; MAGNETIC COUPLINGS; MAGNETIC RELAXATION; NUCLEAR MAGNETIC RESONANCE; PROTEINS; RNA; SPECTROSCOPIC ANALYSIS;

EID: 0042674372     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1090-7807(03)00105-8     Document Type: Article
Times cited : (24)

References (43)
  • 1
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution
    • Tolman J., Flanagan J., Kennedy M., Prestegard J. Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution. Proc. Natl. Acad. Sci. USA. 92:1995;9279-9283.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9279-9283
    • Tolman, J.1    Flanagan, J.2    Kennedy, M.3    Prestegard, J.4
  • 2
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra N., Bax A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science. 278:1997;1111-1114.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 3
    • 0031063544 scopus 로고    scopus 로고
    • 1J(CH) splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra
    • 1J(CH) splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra J. Magn. Reson. 124:1997;512-515.
    • (1997) J. Magn. Reson. , vol.124 , pp. 512-515
    • Tjandra, N.1    Bax, A.2
  • 7
    • 0030236298 scopus 로고    scopus 로고
    • 1H one-bond couplings in proteins using accordion heteronuclear-shift-correlation experiments
    • 1H one-bond couplings in proteins using accordion heteronuclear-shift-correlation experiments J. Magn. Reson. Ser. B. 112:1996;269-274.
    • (1996) J. Magn. Reson. Ser. B. , vol.112 , pp. 269-274
    • Tolman, J.R.1    Prestegard, J.H.2
  • 10
    • 0036008168 scopus 로고    scopus 로고
    • A spin-state-selective experiment for measuring heteronuclear one-bond and homonuclear two-bond couplings from an HSQC-type spectrum
    • Permi P. A spin-state-selective experiment for measuring heteronuclear one-bond and homonuclear two-bond couplings from an HSQC-type spectrum. J. Biomol. NMR. 22:2002;27-35.
    • (2002) J. Biomol. NMR , vol.22 , pp. 27-35
    • Permi, P.1
  • 11
  • 12
    • 0034744427 scopus 로고    scopus 로고
    • 31P dipolar couplings in a DNA oligonucleotide by constant-time NOESY difference spectroscopy
    • 31P dipolar couplings in a DNA oligonucleotide by constant-time NOESY difference spectroscopy J. Biomol. NMR. 19:2001;367-370.
    • (2001) J. Biomol. NMR , vol.19 , pp. 367-370
    • Wu, Z.R.1    Tjandra, N.2    Bax, A.3
  • 13
    • 0036008170 scopus 로고    scopus 로고
    • A novel PH-CT-COSY methodology for measuring J(PH) coupling constants in unlabeled nucleic acids. Application to HIV-2 TAR RNA
    • Carlomagno T., Hennig M., Williamson J.R. A novel PH-CT-COSY methodology for measuring J(PH) coupling constants in unlabeled nucleic acids. Application to HIV-2 TAR RNA. J. Biomol. NMR. 22:2002;65-81.
    • (2002) J. Biomol. NMR , vol.22 , pp. 65-81
    • Carlomagno, T.1    Hennig, M.2    Williamson, J.R.3
  • 14
    • 0035743046 scopus 로고    scopus 로고
    • 3E-E.COSY methods for the measurement of F-19 associated scalar and dipolar coupling constants
    • 3E-E.COSY methods for the measurement of F-19 associated scalar and dipolar coupling constants J. Magn. Reson. 152:2001;179-184.
    • (2001) J. Magn. Reson. , vol.152 , pp. 179-184
    • Luy, B.1    Barchi, J.J.2    Marino, J.P.3
  • 16
    • 0032185144 scopus 로고    scopus 로고
    • Measurement of dipolar couplings for methylene and methyl sites in weakly oriented macromolecules and their use in structure determination
    • Ottiger M., Delaglio F., Marquardt J.L., Tjandra N., Bax A. Measurement of dipolar couplings for methylene and methyl sites in weakly oriented macromolecules and their use in structure determination. J. Magn. Reson. 134:1998;365-369.
    • (1998) J. Magn. Reson. , vol.134 , pp. 365-369
    • Ottiger, M.1    Delaglio, F.2    Marquardt, J.L.3    Tjandra, N.4    Bax, A.5
  • 17
    • 0032538016 scopus 로고    scopus 로고
    • 1H dipolar couplings in NMR spectra of field oriented oligosaccharides
    • 1H dipolar couplings in NMR spectra of field oriented oligosaccharides J. Am. Chem. Soc. 120:1998;9366-9367.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9366-9367
    • Bolon, P.J.1    Prestegard, J.H.2
  • 19
    • 0033603869 scopus 로고    scopus 로고
    • Intensity-based measurement of homonuclear residual dipolar couplings from CT-COSY
    • Tian F., Bolon P.J., Prestegard J.H. Intensity-based measurement of homonuclear residual dipolar couplings from CT-COSY. J. Am. Chem. Soc. 121:1999;7712-7713.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7712-7713
    • Tian, F.1    Bolon, P.J.2    Prestegard, J.H.3
  • 20
    • 0033626533 scopus 로고    scopus 로고
    • Direct measurement of H-1-H-1 dipolar couplings in proteins: A complement to traditional NOE measurements
    • Tian F., Fowler C.A., Zartler E.R., Jenney F.A., Adams M.W., Prestegard J.H. Direct measurement of H-1-H-1 dipolar couplings in proteins: a complement to traditional NOE measurements. J. Biomol. NMR. 18:2000;23-31.
    • (2000) J. Biomol. NMR , vol.18 , pp. 23-31
    • Tian, F.1    Fowler, C.A.2    Zartler, E.R.3    Jenney, F.A.4    Adams, M.W.5    Prestegard, J.H.6
  • 21
    • 0034132563 scopus 로고    scopus 로고
    • Direct refinement against proton-proton dipolar couplings in NMR structure determination of macromolecules
    • Tjandra N., Marquardt J., Clore G.M. Direct refinement against proton-proton dipolar couplings in NMR structure determination of macromolecules. J. Magn. Reson. 142:2000;393-396.
    • (2000) J. Magn. Reson. , vol.142 , pp. 393-396
    • Tjandra, N.1    Marquardt, J.2    Clore, G.M.3
  • 22
    • 0034716747 scopus 로고    scopus 로고
    • Measurement of magnitude and sign of H,H-dipolar couplings in proteins
    • Peti W., Griesinger C. Measurement of magnitude and sign of H,H-dipolar couplings in proteins. J. Am. Chem. Soc. 122:2000;3975-3976.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3975-3976
    • Peti, W.1    Griesinger, C.2
  • 24
    • 0037151670 scopus 로고    scopus 로고
    • 1H dipolar couplings in weakly aligned proteins
    • 1H dipolar couplings in weakly aligned proteins J. Am. Chem. Soc. 124:2002;9672-9673.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 9672-9673
    • Wu, Z.R.1    Bax, A.2
  • 25
    • 0030612335 scopus 로고    scopus 로고
    • Use of dipolar H-1-N-15 and H-1-C-13 couplings in the structure determination of magnetically oriented macromolecules in solution
    • Tjandra N., Omichinski J.G., Gronenborn A.M., Clore G.M., Bax A. Use of dipolar H-1-N-15 and H-1-C-13 couplings in the structure determination of magnetically oriented macromolecules in solution. Nat. Struct. Biol. 4:1997;732-738.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 732-738
    • Tjandra, N.1    Omichinski, J.G.2    Gronenborn, A.M.3    Clore, G.M.4    Bax, A.5
  • 26
    • 0031244139 scopus 로고    scopus 로고
    • High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium
    • Bax A., Tjandra N. High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium. J. Biomol. NMR. 10:1997;289-292.
    • (1997) J. Biomol. NMR , vol.10 , pp. 289-292
    • Bax, A.1    Tjandra, N.2
  • 27
    • 0034146355 scopus 로고    scopus 로고
    • Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times
    • Kontaxis G., Clore G.M., Bax A. Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times. J. Magn. Reson. 143:2000;184-196.
    • (2000) J. Magn. Reson. , vol.143 , pp. 184-196
    • Kontaxis, G.1    Clore, G.M.2    Bax, A.3
  • 28
    • 0031174215 scopus 로고    scopus 로고
    • 1J(XH)-resolved E.COSY-type measurement of heteronuclear coupling constants in proteins
    • 1J(XH)-resolved E.COSY-type measurement of heteronuclear coupling constants in proteins J. Biomol. NMR. 10:1997;89-94.
    • (1997) J. Biomol. NMR , vol.10 , pp. 89-94
    • Meissner, A.1    Duus, J.O.2    Sørensen, O.W.3
  • 29
    • 0002473875 scopus 로고    scopus 로고
    • Spin-state-selective excitation. Application for E.COSY-type measurement of J(HH) coupling constants
    • Meissner A., Duus J.O., Sørensen O.W. Spin-state-selective excitation. Application for E.COSY-type measurement of J(HH) coupling constants. J. Magn. Reson. 128:1997;92-97.
    • (1997) J. Magn. Reson. , vol.128 , pp. 92-97
    • Meissner, A.1    Duus, J.O.2    Sørensen, O.W.3
  • 30
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger M., Delaglio F., Bax A. Measurement of. J and dipolar couplings from simplified two-dimensional NMR spectra J. Magn. Reson. 131:1998;373-378.
    • (1998) J. Magn. Reson. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 33
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T-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
    • Pervushin K., Riek R., Wider G., Wüthrich K. Attenuated T-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. 94:1997;12366-12371.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 34
    • 0032126855 scopus 로고    scopus 로고
    • Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in C-13-labeled proteins
    • Pervushin K., Riek R., Wider G., Wüthrich K. Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in C-13-labeled proteins. J. Am. Chem. Soc. 120:1998;6394-6400.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6394-6400
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wüthrich, K.4
  • 35
    • 0042896698 scopus 로고
    • Modulated spin echo trains from liquid crystals
    • Vold R.L., Chan S.O. Modulated spin echo trains from liquid crystals. J. Chem. Phys. 53:1970;449-451.
    • (1970) J. Chem. Phys. , vol.53 , pp. 449-451
    • Vold, R.L.1    Chan, S.O.2
  • 36
    • 51149218559 scopus 로고
    • High-resolution study of NMR spin echoes: "J-Spectra"
    • Freeman R., Hill H.D.W. High-resolution study of NMR spin echoes: "J-Spectra" J. Chem. Phys. 54:1971;301-313.
    • (1971) J. Chem. Phys. , vol.54 , pp. 301-313
    • Freeman, R.1    Hill, H.D.W.2
  • 37
    • 0006681995 scopus 로고
    • Two-dimensional J-spectroscopy: Proton-coupled carbon-13 NMR
    • Bodenhausen G., Freeman R., Turner D.L. Two-dimensional J-spectroscopy: proton-coupled carbon-13 NMR. J. Chem. Phys. 65:1976;839-840.
    • (1976) J. Chem. Phys. , vol.65 , pp. 839-840
    • Bodenhausen, G.1    Freeman, R.2    Turner, D.L.3
  • 38
    • 36749114535 scopus 로고
    • Homonuclear broad band decoupling and two-dimensional J-resolved NMR spectroscopy
    • Aue W.P., Ernst R.R. Homonuclear broad band decoupling and two-dimensional J-resolved NMR spectroscopy. J. Chem. Phys. 64:1976;4226-4227.
    • (1976) J. Chem. Phys. , vol.64 , pp. 4226-4227
    • Aue, W.P.1    Ernst, R.R.2
  • 39
    • 0000960167 scopus 로고
    • A convenient technique for the measurement and assignment of long-range C-13 proton coupling-constants
    • Keeler J., Neuhaus D., Titman J.J. A convenient technique for the measurement and assignment of long-range C-13 proton coupling-constants. Chem. Phys. Lett. 146:1988;545-548.
    • (1988) Chem. Phys. Lett. , vol.146 , pp. 545-548
    • Keeler, J.1    Neuhaus, D.2    Titman, J.J.3
  • 40
    • 0032556228 scopus 로고    scopus 로고
    • Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments
    • Weigelt J. Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments. J. Am. Chem. Soc. 120:1998;10778-10779.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 10778-10779
    • Weigelt, J.1
  • 42
    • 44049118414 scopus 로고
    • A constant time HSQC experiment
    • Santoro J., King G. A constant time HSQC experiment. J. Magn. Reson. 97:1992;202-207.
    • (1992) J. Magn. Reson. , vol.97 , pp. 202-207
    • Santoro, J.1    King, G.2
  • 43
    • 0033637980 scopus 로고    scopus 로고
    • Impact of transverse relaxation optimized spectroscopy (TROSY) on NMR as a technique in structural biology
    • Pervushin K. Impact of transverse relaxation optimized spectroscopy (TROSY) on NMR as a technique in structural biology. Quart. Rev. Biophys. 33:2000;161-197.
    • (2000) Quart. Rev. Biophys. , vol.33 , pp. 161-197
    • Pervushin, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.