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Volumn 20, Issue 4, 2006, Pages 153-167

Single scan TROSY and E.COSY suite of experiments for the measurement of residual dipolar couplings in proteins

Author keywords

eCOSY; NMR; Residual dipolar couplings; TROSY

Indexed keywords

MODIFICATION; MODULATION; SPECTROSCOPY; WATER;

EID: 33845432425     PISSN: 07124813     EISSN: None     Source Type: Journal    
DOI: 10.1155/2006/812107     Document Type: Article
Times cited : (2)

References (25)
  • 1
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • A. Bax and A. Grishaev, Weak alignment NMR: a hawk-eyed view of biomolecular structure, Curr. Opin. Struct. Biol. 15 (2005), 563-570.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 2
    • 0034919243 scopus 로고    scopus 로고
    • Dipolar couplings in macromolecular structure determination
    • A. Bax, G. Kontaxis and N. Tjandra, Dipolar couplings in macromolecular structure determination, Methods Enzymol. 339 (2001), 127-174.
    • (2001) Methods Enzymol. , vol.339 , pp. 127-174
    • Bax, A.1    Kontaxis, G.2    Tjandra, N.3
  • 4
    • 16244419326 scopus 로고    scopus 로고
    • Determination of protein backbone structures from residual dipolar couplings
    • J.H. Prestegard, K.L. Mayer, H. Valafar and G.C. Benison, Determination of protein backbone structures from residual dipolar couplings, Methods Enzymol. 394 (2005), 175-209.
    • (2005) Methods Enzymol. , vol.394 , pp. 175-209
    • Prestegard, J.H.1    Mayer, K.L.2    Valafar, H.3    Benison, G.C.4
  • 6
    • 0031063544 scopus 로고    scopus 로고
    • 1JCH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra
    • 1JCH 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
    • 0030018695 scopus 로고    scopus 로고
    • 15N-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling
    • 15N-enriched human ubiquitin resulting from relaxation interference and residual dipolar coupling, J. Am. Chem. Soc. 118 (1996), 6264-6272.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6264-6272
    • Tjandra, N.1    Grzesiek, S.2    Bax, A.3
  • 8
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • M. Ottiger, F. Delaglio and A. Bax, Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra, J. Magn. Reson. 131 (1998), 367-372.
    • (1998) J. Magn. Reson. , vol.131 , pp. 367-372
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 9
    • 0032174606 scopus 로고    scopus 로고
    • Spin-state selection filters fort he measurement of heteronuclear one-bond coupling constants
    • P. Andersson, J.Weigelt and G. Otting, Spin-state selection filters fort he measurement of heteronuclear one-bond coupling constants, J. Biomol. NMR 12 (1998), 435-441.
    • (1998) J. Biomol. NMR , vol.12 , pp. 435-441
    • Andersson, P.1    Weigelt, J.2    Otting, G.3
  • 10
    • 0035743660 scopus 로고    scopus 로고
    • Accurate measurement of small spin-spin couplings in partially aligned molecules using a novel J-mismatch compensated spin-state-selection filter
    • B. Brutscher, Accurate measurement of small spin-spin couplings in partially aligned molecules using a novel J-mismatch compensated spin-state-selection filter, J. Magn. Reson. 151 (2001), 332-338.
    • (2001) J. Magn. Reson. , vol.151 , pp. 332-338
    • Brutscher, B.1
  • 11
    • 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 (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
  • 12
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • L. Kay, P. Keifer and 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.1    Keifer, P.2    Saarinen, T.3
  • 13
    • 0032162021 scopus 로고    scopus 로고
    • Sensitivity enhancement in the TROSY experiment
    • M. Czisch and R. Boelens, Sensitivity enhancement in the TROSY experiment, J. Magn. Reson. 134 (1998), 158-160.
    • (1998) J. Magn. Reson. , vol.134 , pp. 158-160
    • Czisch, M.1    Boelens, R.2
  • 14
    • 0032556228 scopus 로고    scopus 로고
    • Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments
    • J.Weigelt, 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
  • 15
    • 0000867858 scopus 로고    scopus 로고
    • Single transition-to-single transition polarization transfer (ST2-PT) in [15N,1H]-TROSY
    • K.V. Pervushin, G. Wider and K. Wüthrich, Single transition-to-single transition polarization transfer (ST2-PT) in [15N,1H]-TROSY, J. Biomol. NMR 12 (1998), 345-348.
    • (1998) J. Biomol. NMR , vol.12 , pp. 345-348
    • Pervushin, K.V.1    Wider, G.2    Wüthrich, K.3
  • 17
    • 33646899398 scopus 로고    scopus 로고
    • NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid binding protein
    • L. Ragona, M. Catalano, M. Luppi, D. Cicero, T. Eliseo, J. Foote, F. Fogolari, L. Zetta and H. Molinari, NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid binding protein, J. Biol. Chem. 281 (2006), 9697-9709.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9697-9709
    • Ragona, L.1    Catalano, M.2    Luppi, M.3    Cicero, D.4    Eliseo, T.5    Foote, J.6    Fogolari, F.7    Zetta, L.8    Molinari, H.9
  • 18
    • 33845426649 scopus 로고    scopus 로고
    • Backbone NMR assignment of the 29.6 kDa Rhodanese protein from Azotobacter vinelandii
    • in press
    • M. Gallo, S. Melino, R. Melis, M. Paci and D.O. Cicero, Backbone NMR assignment of the 29.6 kDa Rhodanese protein from Azotobacter vinelandii, J. Biomol. NMR (2006), in press.
    • (2006) J. Biomol. NMR
    • Gallo, M.1    Melino, S.2    Melis, R.3    Paci, M.4    Cicero, D.O.5
  • 20
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • B.A. Johnson and R.A. Blevins, NMRView: A computer program for the visualization and analysis of NMR data, J. Biomol. NMR 4 (1994), 603-661.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-661
    • Johnson, B.A.1    Blevins, R.A.2
  • 21
    • 0031760503 scopus 로고    scopus 로고
    • Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
    • M.R. Hansen, L. Mueller and A. Pardi, Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions, Nat. Struct. Biol. 5 (1998), 1065-1074.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1065-1074
    • Hansen, M.R.1    Mueller, L.2    Pardi, A.3
  • 22
    • 0032622242 scopus 로고    scopus 로고
    • Sensitivity improvement of transverse relaxation-optimized spectroscopy
    • M. Rance, L.J. Patrick and A.G. Palmer III, Sensitivity improvement of transverse relaxation-optimized spectroscopy, J. Magn. Reson. 136 (1999), 92-101.
    • (1999) J. Magn. Reson. , vol.136 , pp. 92-101
    • Rance, M.1    Patrick, L.J.2    Palmer III, A.G.3
  • 25
    • 0034183497 scopus 로고    scopus 로고
    • Clean TROSY: Compensation for relaxation-induced artifacts
    • T. Schulte-Herbrüggen and O.W. Sørensen, Clean TROSY: compensation for relaxation-induced artifacts, J. Magn. Reson. 144 (2000), 123-128.
    • (2000) J. Magn. Reson. , vol.144 , pp. 123-128
    • Schulte-Herbrüggen, T.1    Sørensen, O.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.