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Volumn 51, Issue 1-2, 2011, Pages 89-103

Measurement of 1H- 15N and 1H- 13C residual dipolar couplings in nucleic acids from TROSY intensities

Author keywords

A form RNA; ARTSY; BEST; DNA; Quantitative J correlation; RDC; RNA; TROSY

Indexed keywords

ADENINE; AMINO ACID; CARBON 13; HYDROGEN; HYDROXYL GROUP; NITROGEN 15; NUCLEIC ACID;

EID: 80755181371     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-011-9544-y     Document Type: Article
Times cited : (22)

References (60)
  • 1
    • 0000302902 scopus 로고    scopus 로고
    • An α/β-HSQC-α/β Experiment for Spin-State Selective Editing of IS Cross Peaks
    • P Andersson A Annila G Otting 1998 An alpha/beta-HSQC-alpha/beta experiment for spin-state selective editing of IS cross peaks J Magn Reson 133 364 367 1998JMagR.133..364A 10.1006/jmre.1998.1492 (Pubitemid 128450653)
    • (1998) Journal of Magnetic Resonance , vol.133 , Issue.2 , pp. 364-367
    • Andersson, P.1    Annila, A.2    Otting, G.3
  • 2
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • DOI 10.1016/j.sbi.2005.08.006, PII S0959440X05001545, Carbohydrates and Glycoconjugates/Biophysical Methods
    • A Bax A Grishaev 2005 Weak alignment NMR: a hawk-eyed view of biomolecular structure Curr Opin Struct Biol 15 563 570 10.1016/j.sbi.2005.08. 006 (Pubitemid 41393488)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 3
    • 33644757144 scopus 로고
    • Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR
    • 10.1016/0022-2364(83)90241-X
    • A Bax RH Griffey BL Hawkins 1983 Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR J Magn Reson 55 301 315 10.1016/0022-2364(83)90241-X
    • (1983) J Magn Reson , vol.55 , pp. 301-315
    • Bax, A.1    Griffey, R.H.2    Hawkins, B.L.3
  • 4
    • 75849123605 scopus 로고    scopus 로고
    • Measurement and interpretation of N-15-H-1 residual dipolar couplings in larger proteins
    • 2010JMagR.203.11B 10.1016/j.jmr.2009.11.014
    • A Bhattacharya M Revington ERP Zuiderweg 2010 Measurement and interpretation of N-15-H-1 residual dipolar couplings in larger proteins J Magn Reson 203 11 28 2010JMagR.203...11B 10.1016/j.jmr.2009.11.014
    • (2010) J Magn Reson , vol.203 , pp. 11-28
    • Bhattacharya, A.1    Revington, M.2    Zuiderweg, E.R.P.3
  • 5
    • 0032842695 scopus 로고    scopus 로고
    • 13C spin relaxation measurements in RNA: Sensitivity and resolution improvement using spin-state selective correlation experiments
    • DOI 10.1023/A:1008365712799
    • J Boisbouvier B Brutscher JP Simorre D Marion 1999 C-13 spin relaxation measurements in RNA: Sensitivity and resolution improvement using spin-state selective correlation experiments J Biomol NMR 14 241 252 10.1023/A: 1008365712799 (Pubitemid 29396483)
    • (1999) Journal of Biomolecular NMR , vol.14 , Issue.3 , pp. 241-252
    • Boisbouvier, J.1    Brutscher, B.2    Simorre, J.-P.3    Marion, D.4
  • 8
    • 0001331889 scopus 로고    scopus 로고
    • Thermal offset viscosities of liquid H2O, D2O, and T2O
    • 10.1021/jp9842953
    • CH Cho J Urquidi S Singh GW Robinson 1999 Thermal offset viscosities of liquid H2O, D2O, and T2O J Phys Chem B 103 1991 1994 10.1021/jp9842953
    • (1999) J Phys Chem B , vol.103 , pp. 1991-1994
    • Cho, C.H.1    Urquidi, J.2    Singh, S.3    Robinson, G.W.4
  • 9
    • 0034254909 scopus 로고    scopus 로고
    • Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear overhauser enhancement data and dipolar couplings by rigid body minimization
    • DOI 10.1073/pnas.97.16.9021
    • GM Clore 2000 Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization Proc Natl Acad Sci USA 97 9021 9025 2000PNAS...97.9021C 10.1073/pnas.97.16.9021 (Pubitemid 30626666)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.16 , pp. 9021-9025
    • Clore, G.M.1
  • 10
    • 33745358903 scopus 로고    scopus 로고
    • Interference between cross-correlated relaxation and the measurement of scalar and dipolar couplings by Quantitative J
    • DOI 10.1007/s10858-006-0028-4
    • E de Alba N Tjandra 2006 Interference between cross-correlated relaxation and the measurement of scalar and dipolar couplings by quantitative J J Biomol NMR 35 1 16 10.1007/s10858-006-0028-4 (Pubitemid 43941719)
    • (2006) Journal of Biomolecular NMR , vol.35 , Issue.1 , pp. 1-16
    • De Alba, E.1    Tjandra, N.2
  • 11
    • 33750610579 scopus 로고    scopus 로고
    • 1H couplings in proteins: Effects of cross-correlated relaxation, selective pulses and dynamic frequency shifts
    • DOI 10.1016/j.jmr.2006.08.003, PII S1090780706002461
    • E de Alba N Tjandra 2006 On the accurate measurement of amide one-bond N-15-H-1 couplings in proteins: Effects of cross-correlated relaxation, selective pulses and dynamic frequency shifts J Magn Reson 183 160 165 2006JMagR.183..160A 10.1016/j.jmr.2006.08.003 (Pubitemid 44692528)
    • (2006) Journal of Magnetic Resonance , vol.183 , Issue.1 , pp. 160-165
    • Alba, E.D.1    Tjandra, N.2
  • 12
    • 0029400480 scopus 로고
    • NMRpipe-a multidimensional spectral processing system based on Unix pipes
    • 10.1007/BF00197809
    • F Delaglio S Grzesiek GW Vuister G Zhu J Pfeifer A Bax 1995 NMRpipe-a multidimensional spectral processing system based on Unix pipes J Biomol NMR 6 277 293 10.1007/BF00197809
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 13
    • 0034801402 scopus 로고    scopus 로고
    • 2H-labeled proteins: Application to domain orientation in maltose binding protein
    • DOI 10.1021/ja003833y
    • J Evenas A Mittermaier DW Yang LE Kay 2001 Measurement of C-13(alpha)-C-13(beta) dipolar couplings in N- 15, C-13, H-2-labeled proteins: Application to domain orientation in maltose binding protein J Am Chem Soc 123 2858 2864 10.1021/ja003833y (Pubitemid 32910712)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.12 , pp. 2858-2864
    • Evenas, J.1    Mittermaier, A.2    Yang, D.3    Kay, L.E.4
  • 14
    • 67650525076 scopus 로고    scopus 로고
    • Longitudinal-Relaxation-Enhanced NMR Experiments for the Study of Nucleic Acids in Solution
    • 10.1021/ja901633y
    • J Farjon J Boisbouvier P Schanda A Pardi JP Simorre B Brutscher 2009 Longitudinal-Relaxation-Enhanced NMR Experiments for the Study of Nucleic Acids in Solution J Am Chem Soc 131 8571 8577 10.1021/ja901633y
    • (2009) J Am Chem Soc , vol.131 , pp. 8571-8577
    • Farjon, J.1    Boisbouvier, J.2    Schanda, P.3    Pardi, A.4    Simorre, J.P.5    Brutscher, B.6
  • 15
    • 78149362336 scopus 로고    scopus 로고
    • Facile measurement of H-1-N-15 residual dipolar couplings in larger perdeuterated proteins
    • 10.1007/s10858-010-9441-9
    • NC Fitzkee A Bax 2010 Facile measurement of H-1-N-15 residual dipolar couplings in larger perdeuterated proteins J Biomol NMR 48 65 70 10.1007/s10858-010-9441-9
    • (2010) J Biomol NMR , vol.48 , pp. 65-70
    • Fitzkee, N.C.1    Bax, A.2
  • 16
    • 49149148488 scopus 로고
    • Radiofrequency pulse sequences which compensate their own imperfections
    • 10.1016/0022-2364(80)90327-3
    • R Freeman SP Kempsell MH Levitt 1980 Radiofrequency pulse sequences which compensate their own imperfections J Magn Reson 38 453 479 10.1016/0022- 2364(80)90327-3
    • (1980) J Magn Reson , vol.38 , pp. 453-479
    • Freeman, R.1    Kempsell, S.P.2    Levitt, M.H.3
  • 17
    • 44949280676 scopus 로고
    • Band-selective radiofrequency pulses
    • 10.1016/0022-2364(91)90034-Q
    • H Geen R Freeman 1991 Band-selective radiofrequency pulses J Magn Reson 93 93 141 10.1016/0022-2364(91)90034-Q
    • (1991) J Magn Reson , vol.93 , pp. 93-141
    • Geen, H.1    Freeman, R.2
  • 18
    • 54049155019 scopus 로고    scopus 로고
    • Solution structure of tRNA(Val) from refinement of homology model against residual dipolar coupling and SAXS data
    • 10.1007/s10858-008-9267-x
    • A Grishaev J Ying MD Canny A Pardi A Bax 2008 Solution structure of tRNA(Val) from refinement of homology model against residual dipolar coupling and SAXS data J Biomol NMR 42 99 109 10.1007/s10858-008-9267-x
    • (2008) J Biomol NMR , vol.42 , pp. 99-109
    • Grishaev, A.1    Ying, J.2    Canny, M.D.3    Pardi, A.4    Bax, A.5
  • 19
    • 67650468450 scopus 로고    scopus 로고
    • Chemical Shift Anisotropy of Imino N-15 Nuclei in Watson-Crick Base Pairs from Magic Angle Spinning Liquid Crystal NMR and Nuclear Spin Relaxation
    • 10.1021/ja903244s
    • A Grishaev LS Yao JF Ying A Pardi A Bax 2009 Chemical Shift Anisotropy of Imino N-15 Nuclei in Watson-Crick Base Pairs from Magic Angle Spinning Liquid Crystal NMR and Nuclear Spin Relaxation J Am Chem Soc 131 9490 9492 10.1021/ja903244s
    • (2009) J Am Chem Soc , vol.131 , pp. 9490-9492
    • Grishaev, A.1    Yao, L.S.2    Ying, J.F.3    Pardi, A.4    Bax, A.5
  • 20
    • 46049083589 scopus 로고    scopus 로고
    • α dipolar couplings of invisible protein states by spin-state selective relaxation dispersion NMR spectroscopy
    • DOI 10.1021/ja801005n
    • DF Hansen P Vallurupalli LE Kay 2008 Quantifying two-bond (HN)-H-1-(CO)-C-13 and one-bond H-1(alpha)-C-13(alpha) dipolar couplings of invisible protein states by spin-state selective relaxation dispersion NMR spectroscopy J Am Chem Soc 130 8397 8405 10.1021/ja801005n (Pubitemid 351898560)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.26 , pp. 8397-8405
    • Hansen, D.F.1    Vallurupalli, P.2    Kay, L.E.3
  • 21
    • 46949093335 scopus 로고    scopus 로고
    • Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states
    • 10.1007/s10858-008-9251-5
    • DF Hansen P Vallurupalli LE Kay 2008 Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states J Biomol NMR 41 113 120 10.1007/s10858-008-9251-5
    • (2008) J Biomol NMR , vol.41 , pp. 113-120
    • Hansen, D.F.1    Vallurupalli, P.2    Kay, L.E.3
  • 22
    • 0030631673 scopus 로고    scopus 로고
    • Broadband Adiabatic Refocusing without Phase Distortion
    • TL Hwang PCM van Zijl M Garwood 1997 Broadband adiabatic refocusing without phase distortion J Magn Reson 124 250 254 1997JMagR.124..250H 10.1006/jmre.1996.1049 (Pubitemid 127451413)
    • (1997) Journal of Magnetic Resonance , vol.124 , Issue.1 , pp. 250-254
    • Hwang, T.-L.1    Van Zijl, P.C.M.2    Garwood, M.3
  • 23
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • 10.1021/ja00052a088
    • LE Kay P Keifer T Saarinen 1992 Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity J Am Chem Soc 114 10663 10665 10.1021/ja00052a088
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 24
    • 0034146355 scopus 로고    scopus 로고
    • Evaluation of cross-correlation effects and measurement of one- bond couplings in proteins with short transverse relaxation times
    • 2000JMagR.143.184K 10.1006/jmre.1999.1979
    • G Kontaxis GM Clore A Bax 2000 Evaluation of cross-correlation effects and measurement of one- bond couplings in proteins with short transverse relaxation times J Magn Reson 143 184 196 2000JMagR.143..184K 10.1006/jmre.1999.1979
    • (2000) J Magn Reson , vol.143 , pp. 184-196
    • Kontaxis, G.1    Clore, G.M.2    Bax, A.3
  • 25
    • 0034794444 scopus 로고    scopus 로고
    • Improving the accuracy of NMR structures of DNA by means of a database potential of mean force describing base-base positional interactions
    • DOI 10.1021/ja010033u
    • J Kuszewski C Schwieters GM Clore 2001 Improving the accuracy of NMR structures of DNA by means of a database potential of mean force describing base-base positional interactions J Am Chem Soc 123 3903 3918 10.1021/ja010033u (Pubitemid 32899477)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.17 , pp. 3903-3918
    • Kuszewski, J.1    Schwieters, C.2    Clore, G.M.3
  • 26
    • 34250159870 scopus 로고    scopus 로고
    • A set of BEST triple-resonance experiments for time-optimized protein resonance assignment
    • DOI 10.1016/j.jmr.2007.04.002, PII S1090780707001103
    • E Lescop P Schanda B Brutscher 2007 A set of BEST triple-resonance experiments for time-optimized protein resonance assignment J Magn Reson 187 163 169 2007JMagR.187..163L 10.1016/j.jmr.2007.04.002 (Pubitemid 46898871)
    • (2007) Journal of Magnetic Resonance , vol.187 , Issue.1 , pp. 163-169
    • Lescop, E.1    Schanda, P.2    Brutscher, B.3
  • 27
    • 49149138125 scopus 로고
    • Compensation for pulse imperfections in NMR spin-echo experiments
    • 10.1016/0022-2364(81)90082-2
    • MH Levitt R Freeman 1981 Compensation for pulse imperfections in NMR spin-echo experiments J Magn Reson 43 65 80 10.1016/0022-2364(81)90082-2
    • (1981) J Magn Reson , vol.43 , pp. 65-80
    • Levitt, M.H.1    Freeman, R.2
  • 28
    • 0033145058 scopus 로고    scopus 로고
    • Order Matrix Analysis of Residual Dipolar Couplings Using Singular Value Decomposition
    • JA Losonczi M Andrec MWF Fischer JH Prestegard 1999 Order matrix analysis of residual dipolar couplings using singular value decomposition J Magn Reson 138 334 342 1999JMagR.138..334L 10.1006/jmre.1999.1754 (Pubitemid 129608294)
    • (1999) Journal of Magnetic Resonance , vol.138 , Issue.2 , pp. 334-342
    • Losonczi, J.A.1    Andrec, M.2    Fischer, M.W.F.3    Prestegard, J.H.4
  • 29
    • 77954759580 scopus 로고    scopus 로고
    • MQ-HNCO-TROSY for the measurement of scalar and residual dipolar couplings in larger proteins: Application to a 557-residue IgFLNa16-21
    • 10.1007/s10858-010-9422-z
    • S Mantylahti O Koskela P Jiang P Permi 2010 MQ-HNCO-TROSY for the measurement of scalar and residual dipolar couplings in larger proteins: application to a 557-residue IgFLNa16-21 J Biomol NMR 47 183 194 10.1007/s10858-010-9422-z
    • (2010) J Biomol NMR , vol.47 , pp. 183-194
    • Mantylahti, S.1    Koskela, O.2    Jiang, P.3    Permi, P.4
  • 30
    • 0002473875 scopus 로고    scopus 로고
    • HH Coupling Constants
    • A Meissner JO Duus OW Sorensen 1997 Spin-state-selective excitation. Application for E.COSY-type measurement of J(HH) coupling constants J Magn Reson 128 92 97 1997JMagR.128...92M 10.1006/jmre.1997.1213 (Pubitemid 127452138)
    • (1997) Journal of Magnetic Resonance , vol.128 , Issue.1 , pp. 92-97
    • Meissner, A.1    Duus, J.O.2    Sorensen, O.W.3
  • 31
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and Dipolar Couplings from Simplified Two-Dimensional NMR Spectra
    • M Ottiger F Delaglio A Bax 1998 Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra J Magn Reson 131 373 378 1998JMagR.131..373O 10.1006/jmre.1998.1361 (Pubitemid 128450579)
    • (1998) Journal of Magnetic Resonance , vol.131 , Issue.2 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 32
    • 44949276869 scopus 로고
    • Sensitivity improvement in proton-detected 2-dimensional heteronuclear correlation Nmr-spectroscopy
    • 10.1016/0022-2364(91)90036-S
    • AG Palmer J Cavanagh PE Wright M Rance 1991 Sensitivity improvement in proton-detected 2-dimensional heteronuclear correlation Nmr-spectroscopy J Magn Reson 93 151 170 10.1016/0022-2364(91)90036-S
    • (1991) J Magn Reson , vol.93 , pp. 151-170
    • Palmer, A.G.1    Cavanagh, J.2    Wright, P.E.3    Rance, M.4
  • 33
    • 0033919516 scopus 로고    scopus 로고
    • 2H)-labeled proteins
    • DOI 10.1023/A:1008372624615
    • P Permi PR Rosevear A Annila 2000 A set of HNCO-based experiments for measurement of residual dipolar couplings in N-15, C-13, (H-2)-labeled proteins J Biomol NMR 17 43 54 10.1023/A:1008372624615 (Pubitemid 30434837)
    • (2000) Journal of Biomolecular NMR , vol.17 , Issue.1 , pp. 43-54
    • Permi, P.1    Rosevear, P.R.2    Annila, A.3
  • 34
    • 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
    • DOI 10.1073/pnas.94.23.12366
    • K Pervushin R Riek G Wider K Wuthrich 1997 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 12366 12371 1997PNAS...9412366P 10.1073/pnas.94.23.12366 (Pubitemid 27492534)
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.23 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 35
    • 0032126855 scopus 로고    scopus 로고
    • 13C-labeled proteins
    • DOI 10.1021/ja980742g
    • K Pervushin R Riek G Wider K Wuthrich 1998 Transverse relaxation-optimized spectroscopy (TROSY) for NMR studies of aromatic spin systems in C-13-labeled proteins J Am Chem Soc 120 6394 6400 10.1021/ja980742g (Pubitemid 28346415)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.25 , pp. 6394-6400
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 36
    • 0000867858 scopus 로고    scopus 로고
    • 1H]-TROSY
    • KV Pervushin G Wider K Wuthrich 1998 Single transition-to-single transition polarization transfer (ST2-PT) in [N15, H1]-TROSY J Biomol NMR 12 345 348 10.1023/A:1008268930690 (Pubitemid 128511298)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.2 , pp. 345-348
    • Pervushin, K.V.1    Wider, G.2    Wuthrich, K.3
  • 37
    • 0037157093 scopus 로고    scopus 로고
    • Model-free analysis of protein backbone motion from residual dipolar couplings
    • DOI 10.1021/ja011883c
    • W Peti J Meiler R Bruschweiler C Griesinger 2002 Model-free analysis of protein backbone motion from residual dipolar couplings J Am Chem Soc 124 5822 5833 10.1021/ja011883c (Pubitemid 34533522)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.20 , pp. 5822-5833
    • Peti, W.1    Meiler, J.2    Bruschweiler, R.3    Griesinger, C.4
  • 38
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous sloutions
    • 10.1007/BF02192855
    • M Piotto V Saudek V Sklenár 1992 Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous sloutions J Biomol NMR 2 661 665 10.1007/BF02192855
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenár, V.3
  • 39
    • 0034480326 scopus 로고    scopus 로고
    • NMR structures of biomolecules using field oriented media and residual dipolar couplings
    • DOI 10.1017/S0033583500003656
    • JH Prestegard HM Al-Hashimi JR Tolman 2000 NMR structures of biomolecules using field oriented media and residual dipolar couplings Q Rev Biophys 33 371 424 10.1017/S0033583500003656 (Pubitemid 32151707)
    • (2000) Quarterly Reviews of Biophysics , vol.33 , Issue.4 , pp. 371-424
    • Prestegard, J.H.1    Al-Hashimi, H.M.2    Tolman, J.R.3
  • 40
    • 33746082442 scopus 로고    scopus 로고
    • Speeding up three-dimensional protein NMR experiments to a few minutes
    • DOI 10.1021/ja062025p
    • P Schanda H Van Melckebeke B Brutscher 2006 Speeding up three-dimensional protein NMR experiments to a few minutes J Am Chem Soc 128 9042 9043 10.1021/ja062025p (Pubitemid 44078980)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.28 , pp. 9042-9043
    • Schanda, P.1    Van Melckebeke, H.2    Brutscher, B.3
  • 41
    • 34548778155 scopus 로고    scopus 로고
    • Ribozymes, riboswitches and beyond: Regulation of gene expression without proteins
    • DOI 10.1038/nrg2172, PII NRG2172
    • A Serganov DJ Patel 2007 Ribozymes, riboswitches and beyond: regulation of gene expression without proteins Nat Rev Genet 8 776 790 10.1038/nrg2172 (Pubitemid 47429208)
    • (2007) Nature Reviews Genetics , vol.8 , Issue.10 , pp. 776-790
    • Serganov, A.1    Patel, D.J.2
  • 42
    • 0033636451 scopus 로고    scopus 로고
    • Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings
    • 10.1023/A:1026501101716
    • NR Skrynnikov LE Kay 2000 Assessment of molecular structure using frame-independent orientational restraints derived from residual dipolar couplings J Biomol NMR 18 239 252 10.1023/A:1026501101716
    • (2000) J Biomol NMR , vol.18 , pp. 239-252
    • Skrynnikov, N.R.1    Kay, L.E.2
  • 43
    • 0034602921 scopus 로고    scopus 로고
    • Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: Differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin
    • 10.1006/jmbi.1999.3430
    • NR Skrynnikov NK Goto DW Yang WY Choy JR Tolman GA Mueller LE Kay 2000 Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: Differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin J Mol Biol 295 1265 1273 10.1006/jmbi.1999.3430
    • (2000) J Mol Biol , vol.295 , pp. 1265-1273
    • Skrynnikov, N.R.1    Goto, N.K.2    Yang, D.W.3    Choy, W.Y.4    Tolman, J.R.5    Mueller, G.A.6    Kay, L.E.7
  • 44
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • DOI 10.1126/science.278.5340.1111
    • N Tjandra A Bax 1997 Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium Science 278 1111 1114 1997Sci...278.1111T 10.1126/science.278.5340.1111 (Pubitemid 27517889)
    • (1997) Science , vol.278 , Issue.5340 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 45
    • 0031063544 scopus 로고    scopus 로고
    • CH Splittings from Magnetic-Field Dependence of J Modulation in Two-Dimensional NMR Spectra
    • N Tjandra A Bax 1997 Measurement of dipolar contributions to (1)J(CH) splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra J Magn Reson 124 512 515 1997JMagR.124..512T 10.1006/jmre.1996.1088 (Pubitemid 127451822)
    • (1997) Journal of Magnetic Resonance , vol.124 , Issue.2 , pp. 512-515
    • Tjandra, N.1    Bax, A.2
  • 46
    • 77954758058 scopus 로고    scopus 로고
    • Major groove width variations in RNA structures determined by NMR and impact of C-13 residual chemical shift anisotropy and H-1-C-13 residual dipolar coupling on refinement
    • 10.1007/s10858-010-9424-x
    • BS Tolbert Y Miyazaki S Barton B Kinde P Starck R Singh A Bax DA Case MF Summers 2010 Major groove width variations in RNA structures determined by NMR and impact of C-13 residual chemical shift anisotropy and H-1-C-13 residual dipolar coupling on refinement J Biomol NMR 47 205 219 10.1007/s10858-010-9424-x
    • (2010) J Biomol NMR , vol.47 , pp. 205-219
    • Tolbert, B.S.1    Miyazaki, Y.2    Barton, S.3    Kinde, B.4    Starck, P.5    Singh, R.6    Bax, A.7    Case, D.A.8    Summers, M.F.9
  • 47
    • 0037048594 scopus 로고    scopus 로고
    • A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy
    • 10.1021/ja0261123
    • JR Tolman 2002 A novel approach to the retrieval of structural and dynamic information from residual dipolar couplings using several oriented media in biomolecular NMR spectroscopy J Am Chem Soc 124 12020 12030 10.1021/ja0261123
    • (2002) J Am Chem Soc , vol.124 , pp. 12020-12030
    • Tolman, J.R.1
  • 48
    • 33646931175 scopus 로고    scopus 로고
    • NMR residual dipolar couplings as probes of biomolecular dynamics
    • DOI 10.1021/cr040429z
    • JR Tolman K Ruan 2006 NMR residual dipolar couplings as probes of biomolecular dynamics Chem Rev 106 1720 1736 10.1021/cr040429z (Pubitemid 43792777)
    • (2006) Chemical Reviews , vol.106 , Issue.5 , pp. 1720-1736
    • Tolman, J.R.1    Ruan, K.2
  • 49
    • 50149085281 scopus 로고    scopus 로고
    • Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy
    • 2008PNAS.10511766V 10.1073/pnas.0804221105
    • P Vallurupalli DF Hansen LE Kay 2008 Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy Proc Natl Acad Sci USA 105 11766 11771 2008PNAS..10511766V 10.1073/pnas.0804221105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11766-11771
    • Vallurupalli, P.1    Hansen, D.F.2    Kay, L.E.3
  • 50
    • 67650828894 scopus 로고    scopus 로고
    • An Analysis of the Effects of H-1(N)-H-1(N) Dipolar Couplings on the Measurement of Amide Bond Vector Orientations in Invisible Protein States by Relaxation Dispersion NMR
    • 10.1021/jp902793y
    • H van Ingen DM Korzhnev LE Kay 2009 An Analysis of the Effects of H-1(N)-H-1(N) Dipolar Couplings on the Measurement of Amide Bond Vector Orientations in Invisible Protein States by Relaxation Dispersion NMR J Phys Chem B 113 9968 9977 10.1021/jp902793y
    • (2009) J Phys Chem B , vol.113 , pp. 9968-9977
    • Van Ingen, H.1    Korzhnev, D.M.2    Kay, L.E.3
  • 51
    • 17644419660 scopus 로고    scopus 로고
    • Simultaneous measurement of protein one-bond residual dipolar couplings without increased resonance overlap
    • DOI 10.1016/j.jmr.2005.02.010, PII S1090780705000340
    • V Vijayan M Zweckstetter 2005 Simultaneous measurement of protein one-bond residual dipolar couplings without increased resonance overlap J Magn Reson 174 245 253 2005JMagR.174..245V 10.1016/j.jmr.2005.02.010 (Pubitemid 40557709)
    • (2005) Journal of Magnetic Resonance , vol.174 , Issue.2 , pp. 245-253
    • Vijayan, V.1    Zweckstetter, M.2
  • 52
    • 70349783815 scopus 로고    scopus 로고
    • A Method for Helical RNA Global Structure Determination in Solution Using Small-Angle X-Ray Scattering and NMR Measurements
    • 10.1016/j.jmb.2009.08.001
    • JB Wang XB Zuo P Yu H Xu MR Starich DM Tiede BA Shapiro CD Schwieters YX Wang 2009 A Method for Helical RNA Global Structure Determination in Solution Using Small-Angle X-Ray Scattering and NMR Measurements J Mol Biol 393 717 734 10.1016/j.jmb.2009.08.001
    • (2009) J Mol Biol , vol.393 , pp. 717-734
    • Wang, J.B.1    Zuo, X.B.2    Yu, P.3    Xu, H.4    Starich, M.R.5    Tiede, D.M.6    Shapiro, B.A.7    Schwieters, C.D.8    Wang, Y.X.9
  • 53
    • 0032850617 scopus 로고    scopus 로고
    • TROSY-based HNCO pulse sequences for the measurement of (1)HN-(15)N, (15)N-(13)CO, (1)HN-(13)CO, (13)CO-(13)C(α) and (1)HN-(13)C(α) dipolar couplings in (15)N, (13)C, (2)H-labeled proteins
    • DOI 10.1023/A:1008314803561
    • DW Yang RA Venters GA Mueller WY Choy LE Kay 1999 TROSY-based HNCO pulse sequences for the measurement of (HN)-H- 1-N-15, N-15-(CO)-C-13, (HN)-H-1-(CO)-C-13, (CO)-C-13-C- 13(alpha) and (HN)-H-1-C-13(alpha) dipolar couplings in N-15, C-13, H-2-labeled proteins J Biomol NMR 14 333 343 10.1023/A:1008314803561 (Pubitemid 29473521)
    • (1999) Journal of Biomolecular NMR , vol.14 , Issue.4 , pp. 333-343
    • Yang, D.1    Venters, R.A.2    Mueller, G.A.3    Choy, W.Y.4    Kay, L.E.5
  • 54
    • 44949168516 scopus 로고    scopus 로고
    • Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis
    • 10.1021/jp0772124
    • L Yao B Vogeli DA Torchia A Bax 2008 Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis J Phys Chem B 112 6045 6056 10.1021/jp0772124
    • (2008) J Phys Chem B , vol.112 , pp. 6045-6056
    • Yao, L.1    Vogeli, B.2    Torchia, D.A.3    Bax, A.4
  • 55
    • 61549122362 scopus 로고    scopus 로고
    • Improved accuracy of N-15-H-1 scalar and residual dipolar couplings from gradient-enhanced IPAP-HSQC experiments on protonated proteins
    • 10.1007/s10858-009-9299-x
    • LS Yao JF Ying A Bax 2009 Improved accuracy of N-15-H-1 scalar and residual dipolar couplings from gradient-enhanced IPAP-HSQC experiments on protonated proteins J Biomol NMR 43 161 170 10.1007/s10858-009-9299-x
    • (2009) J Biomol NMR , vol.43 , pp. 161-170
    • Yao, L.S.1    Ying, J.F.2    Bax, A.3
  • 56
    • 33644841003 scopus 로고    scopus 로고
    • Carbon-13 chemical shift anisotropy in DNA bases from field dependence of solution NMR relaxation rates
    • DOI 10.1002/mrc.1762
    • JF Ying AE Grishaev A Bax 2006 Carbon-13 chemical shift anisotropy in DNA bases from field dependence of solution NMR relaxation rates Magn Reson Chem 44 302 310 10.1002/mrc.1762 (Pubitemid 43363145)
    • (2006) Magnetic Resonance in Chemistry , vol.44 , Issue.3 SPEC. ISS. , pp. 302-310
    • Ying, J.1    Grishaev, A.2    Bax, A.3
  • 57
    • 33947582220 scopus 로고    scopus 로고
    • Mixed-time parallel evolution in multiple quantum NMR experiments: Sensitivity and resolution enhancement in heteronuclear NMR
    • DOI 10.1007/s10858-006-9120-z
    • JF Ying JH Chill JM Louis A Bax 2007 Mixed-time parallel evolution in multiple quantum NMR experiments: sensitivity and resolution enhancement in heteronuclear NMR J Biomol NMR 37 195 204 10.1007/s10858-006-9120-z (Pubitemid 46476997)
    • (2007) Journal of Biomolecular NMR , vol.37 , Issue.3 , pp. 195-204
    • Ying, J.1    Chill, J.H.2    Louis, J.M.3    Bax, A.4
  • 58
    • 34548499333 scopus 로고    scopus 로고
    • Magnetic field induced residual dipolar couplings of imino groups in nucleic acids from measurements at a single magnetic field
    • DOI 10.1007/s10858-007-9181-7
    • JF Ying A Grishaev MP Latham A Pardi A Bax 2007 Magnetic field induced residual dipolar couplings of imino groups in nucleic acids from measurements at a single magnetic field J Biomol NMR 39 91 96 10.1007/s10858-007-9181-7 (Pubitemid 47377482)
    • (2007) Journal of Biomolecular NMR , vol.39 , Issue.2 , pp. 91-96
    • Ying, J.1    Grishaev, A.2    Latham, M.P.3    Pardi, A.4    Bax, A.5
  • 59
    • 31944446215 scopus 로고    scopus 로고
    • Resolving the motional modes that code for RNA adaptation
    • DOI 10.1126/science.1119488
    • Q Zhang XY Sun ED Watt HM Al-Hashimi 2006 Resolving the motional modes that code for RNA adaptation Science 311 653 656 2006Sci...311..653Z 10.1126/science.1119488 (Pubitemid 43191308)
    • (2006) Science , vol.311 , Issue.5761 , pp. 653-656
    • Zhang, Q.1    Sun, X.2    Watt, E.D.3    Al-Hashimi, H.M.4
  • 60
    • 37549017736 scopus 로고    scopus 로고
    • Visualizing spatially correlated dynamics that directs RNA conformational transitions
    • 2007Natur.450.1263Z 10.1038/nature06389
    • Q Zhang AC Stelzer CK Fisher HM Al-Hashimi 2007 Visualizing spatially correlated dynamics that directs RNA conformational transitions Nature 450 1263 1267 2007Natur.450.1263Z 10.1038/nature06389
    • (2007) Nature , vol.450 , pp. 1263-1267
    • Zhang, Q.1    Stelzer, A.C.2    Fisher, C.K.3    Al-Hashimi, H.M.4


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