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Volumn 174, Issue 2, 2005, Pages 245-253

Simultaneous measurement of protein one-bond residual dipolar couplings without increased resonance overlap

Author keywords

CBCA(CO)NH; NMR; Residual dipolar coupling; Scalar coupling; Ubiquitin; Unfolded protein

Indexed keywords

ANISOTROPY; ESCHERICHIA COLI; LIQUID CRYSTALS; MACROMOLECULES; NUCLEAR MAGNETIC RESONANCE; SPECTROSCOPIC ANALYSIS; SPECTRUM ANALYSIS;

EID: 17644419660     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmr.2005.02.010     Document Type: Article
Times cited : (11)

References (40)
  • 4
    • 0034721465 scopus 로고    scopus 로고
    • Alignment of biopolymers in strained gels: A new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR
    • R. Tycko, F.J. Blanco, and Y. Ishii Alignment of biopolymers in strained gels: a new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR J. Am. Chem. Soc. 122 2000 9340 9341
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 9340-9341
    • Tycko, R.1    Blanco, F.J.2    Ishii, Y.3
  • 6
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • N. Tjandra, and A. Bax 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
  • 7
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins-information for structure determination in solution
    • J.R. Tolman, J.M. Flanagan, M.A. Kennedy, and J.H. Prestegard 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.R.1    Flanagan, J.M.2    Kennedy, M.A.3    Prestegard, J.H.4
  • 8
    • 4544229498 scopus 로고    scopus 로고
    • Simultaneous assignment and structure determination of protein backbones by using NMR dipolar couplings
    • Y.S. Jung, M. Sharma, and M. Zweckstetter Simultaneous assignment and structure determination of protein backbones by using NMR dipolar couplings Angew. Chem. Int. Ed. 43 2004 3479 3481
    • (2004) Angew. Chem. Int. Ed. , vol.43 , pp. 3479-3481
    • Jung, Y.S.1    Sharma, M.2    Zweckstetter, M.3
  • 9
    • 0033637553 scopus 로고    scopus 로고
    • Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings
    • J.J. Chou, S.P. Li, and A. Bax Study of conformational rearrangement and refinement of structural homology models by the use of heteronuclear dipolar couplings J. Biomol. NMR 18 2000 217 227
    • (2000) J. Biomol. NMR , vol.18 , pp. 217-227
    • Chou, J.J.1    Li, S.P.2    Bax, A.3
  • 10
    • 0034620764 scopus 로고    scopus 로고
    • Protein structure determination using molecular fragment replacement and NMR dipolar couplings
    • F. Delaglio, G. Kontaxis, and A. Bax Protein structure determination using molecular fragment replacement and NMR dipolar couplings J. Am. Chem. Soc. 122 2000 2142 2143
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2142-2143
    • Delaglio, F.1    Kontaxis, G.2    Bax, A.3
  • 11
    • 0035925135 scopus 로고    scopus 로고
    • Determination of protein backbone structure using only residual dipolar couplings
    • J.C. Hus, D. Marion, and M. Blackledge Determination of protein backbone structure using only residual dipolar couplings J. Am. Chem. Soc. 123 2001 1541 1542
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1541-1542
    • Hus, J.C.1    Marion, D.2    Blackledge, M.3
  • 12
    • 0035979383 scopus 로고    scopus 로고
    • Nuclear magnetic resonance in the era of structural genomics
    • J.H. Prestegard, H. Valafar, J. Glushka, and F. Tian Nuclear magnetic resonance in the era of structural genomics Biochemistry 40 2001 8677 8685
    • (2001) Biochemistry , vol.40 , pp. 8677-8685
    • Prestegard, J.H.1    Valafar, H.2    Glushka, J.3    Tian, F.4
  • 13
    • 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 373 378
    • (1998) J. Magn. Reson. , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 14
    • 0035131780 scopus 로고    scopus 로고
    • Simple multidimensional NMR experiments to obtain different types of one-bond dipolar couplings simultaneously
    • E. de Alba, M. Suzuki, and N. Tjandra Simple multidimensional NMR experiments to obtain different types of one-bond dipolar couplings simultaneously J. Biomol. NMR 19 2001 63 67
    • (2001) J. Biomol. NMR , vol.19 , pp. 63-67
    • De Alba, E.1    Suzuki, M.2    Tjandra, N.3
  • 15
    • 0033919516 scopus 로고    scopus 로고
    • A set of HNCO-based experiments for measurement of residual dipolar couplings in N-15, C-13, (H-2)-labeled proteins
    • P. Permi, P.R. Rosevear, and A. Annila 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 2000 43 54
    • (2000) J. Biomol. NMR , vol.17 , pp. 43-54
    • Permi, P.1    Rosevear, P.R.2    Annila, A.3
  • 16
    • 0035742330 scopus 로고    scopus 로고
    • Methods for the measurement of (1)J(NC alpha) and (2)J(NC alpha) from a simplified 2D C-13(alpha)-coupled N-15 SE-HSQC spectrum
    • S. Heikkinen, P. Permi, and I. Kilpelainen Methods for the measurement of (1)J(NC alpha) and (2)J(NC alpha) from a simplified 2D C-13(alpha)-coupled N-15 SE-HSQC spectrum J. Magn. Reson. 148 2001 53 60
    • (2001) J. Magn. Reson. , vol.148 , pp. 53-60
    • Heikkinen, S.1    Permi, P.2    Kilpelainen, I.3
  • 17
    • 0037330866 scopus 로고    scopus 로고
    • Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [(15)N,(1)H]-TROSY-HNC experiment
    • H.L. Wienk, M.M. Martinez, G.N. Yalloway, J.M. Schmidt, C. Perez, H. Ruterjans, and F. Lohr Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [(15)N,(1)H]-TROSY-HNC experiment J. Biomol. NMR 25 2003 133 145
    • (2003) J. Biomol. NMR , vol.25 , pp. 133-145
    • Wienk, H.L.1    Martinez, M.M.2    Yalloway, G.N.3    Schmidt, J.M.4    Perez, C.5    Ruterjans, H.6    Lohr, F.7
  • 18
    • 0142260977 scopus 로고    scopus 로고
    • Measurement of residual dipolar couplings from H-1(alpha) to C-13(alpha) and N-15 using a simple HNCA-based experiment
    • P. Permi Measurement of residual dipolar couplings from H-1(alpha) to C-13(alpha) and N-15 using a simple HNCA-based experiment J. Biomol. NMR 27 2003 341 349
    • (2003) J. Biomol. NMR , vol.27 , pp. 341-349
    • Permi, P.1
  • 19
    • 0141757463 scopus 로고    scopus 로고
    • Simultaneous and accurate determination of one-bond N-15-C-13' and two-bond H-1(N)-C-13' dipolar couplings
    • K.Y. Ding, and A.M. Gronenborn Simultaneous and accurate determination of one-bond N-15-C-13' and two-bond H-1(N)-C-13' dipolar couplings J. Am. Chem. Soc. 125 2003 11504 11505
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11504-11505
    • Ding, K.Y.1    Gronenborn, A.M.2
  • 20
    • 0032506009 scopus 로고    scopus 로고
    • TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
    • M. Salzmann, K. Pervushin, G. Wider, H. Senn, and K. Wuthrich TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins Proc. Natl. Acad. Sci. USA 95 1998 13585 13590
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13585-13590
    • Salzmann, M.1    Pervushin, K.2    Wider, G.3    Senn, H.4    Wuthrich, K.5
  • 21
    • 0033626526 scopus 로고    scopus 로고
    • Measurement of one-bond N-15-C-13 ' dipolar couplings in medium sized proteins
    • J.J. Chou, F. Delaglio, and A. Bax Measurement of one-bond N-15-C-13 ' dipolar couplings in medium sized proteins J. Biomol. NMR 18 2000 101 105
    • (2000) J. Biomol. NMR , vol.18 , pp. 101-105
    • Chou, J.J.1    Delaglio, F.2    Bax, A.3
  • 22
    • 0032850617 scopus 로고    scopus 로고
    • 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
    • D.W. Yang, R.A. Venters, G.A. Mueller, W.Y. Choy, and L.E. Kay 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 1999 333 343
    • (1999) J. Biomol. NMR , vol.14 , pp. 333-343
    • Yang, D.W.1    Venters, R.A.2    Mueller, G.A.3    Choy, W.Y.4    Kay, L.E.5
  • 23
    • 0033375146 scopus 로고    scopus 로고
    • Robust refocusing of C-13 magnetization in multidimensional NMR experiments by adiabatic fast passage pulses
    • M. Zweckstetter, and T.A. Holak Robust refocusing of C-13 magnetization in multidimensional NMR experiments by adiabatic fast passage pulses J. Biomol. NMR 15 1999 331 334
    • (1999) J. Biomol. NMR , vol.15 , pp. 331-334
    • Zweckstetter, M.1    Holak, T.A.2
  • 24
    • 9444245493 scopus 로고
    • Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance Nmr
    • S. Grzesiek, and A. Bax Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance Nmr J. Am. Chem. Soc. 114 1992 6291 6293
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 25
    • 0034835794 scopus 로고    scopus 로고
    • Protein side-chain rotamers from dipolar couplings in a liquid crystalline phase
    • J.J. Chou, and A. Bax Protein side-chain rotamers from dipolar couplings in a liquid crystalline phase J. Am. Chem. Soc. 123 2001 3844 3845
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3844-3845
    • Chou, J.J.1    Bax, A.2
  • 26
    • 0141531993 scopus 로고    scopus 로고
    • The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli
    • L. Pappalardo, I.G. Janausch, V. Vijayan, E. Zientz, J. Junker, W. Peti, M. Zweckstetter, G. Unden, and C. Griesinger The NMR structure of the sensory domain of the membranous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli J. Biol. Chem. 278 2003 39185 39188
    • (2003) J. Biol. Chem. , vol.278 , pp. 39185-39188
    • Pappalardo, L.1    Janausch, I.G.2    Vijayan, V.3    Zientz, E.4    Junker, J.5    Peti, W.6    Zweckstetter, M.7    Unden, G.8    Griesinger, C.9
  • 27
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • M. Ruckert, and G. Otting Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments J. Am. Chem. Soc. 122 2000 7793 7797
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7793-7797
    • Ruckert, M.1    Otting, G.2
  • 28
    • 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
  • 29
    • 0034852135 scopus 로고    scopus 로고
    • Characterization of molecular alignment in aqueous suspensions of Pf1 bacteriophage
    • M. Zweckstetter, and A. Bax Characterization of molecular alignment in aqueous suspensions of Pf1 bacteriophage J. Biomol. NMR 20 2001 365 377
    • (2001) J. Biomol. NMR , vol.20 , pp. 365-377
    • Zweckstetter, M.1    Bax, A.2
  • 32
    • 0034146355 scopus 로고    scopus 로고
    • Evaluation of cross-correlation effects and measurement of one-bond couplings in proteins with short transverse relaxation times
    • G. Kontaxis, G.M. Clore, and A. Bax 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
  • 33
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • M. Sattler, J. Schleucher, and C. Griesinger Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients Prog. Nucl. Magn. Reson. Spectrosc. 34 1999 93 158
    • (1999) Prog. Nucl. Magn. Reson. Spectrosc. , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 34
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å Resolution
    • S. Vijaykumar, C.E. Bugg, and W.J. Cook Structure of ubiquitin refined at 1.8 Å Resolution J. Mol. Biol. 194 1987 531 544
    • (1987) J. Mol. Biol. , vol.194 , pp. 531-544
    • Vijaykumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 35
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR
    • M. Zweckstetter, and A. Bax Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR J. Am. Chem. Soc. 122 2000 3791 3792
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 36
    • 0000867858 scopus 로고    scopus 로고
    • Single transition-to-single transition polarization transfer (ST2-PT) in N-15,H-1-TROSY
    • K.V. Pervushin, G. Wider, and K. Wuthrich Single transition-to-single transition polarization transfer (ST2-PT) in N-15,H-1-TROSY J. Biomol. NMR 12 1998 345 348
    • (1998) J. Biomol. NMR , vol.12 , pp. 345-348
    • Pervushin, K.V.1    Wider, G.2    Wuthrich, K.3
  • 37
    • 0029270246 scopus 로고
    • Short selective pulses for biochemical applications
    • E. Kupce, J. Boyd, and I.D. Campbell Short selective pulses for biochemical applications J. Magn. Reson. B 106 1995 300 303
    • (1995) J. Magn. Reson. B , vol.106 , pp. 300-303
    • Kupce, E.1    Boyd, J.2    Campbell, I.D.3
  • 38
    • 48549111126 scopus 로고
    • Highly selective Pi/2 and Pi-pulse generation
    • M.S. Silver, R.I. Joseph, and D.I. Hoult Highly selective Pi/2 and Pi-pulse generation J. Magn. Reson. 59 1984 347 351
    • (1984) J. Magn. Reson. , vol.59 , pp. 347-351
    • Silver, M.S.1    Joseph, R.I.2    Hoult, D.I.3
  • 39
    • 0002426603 scopus 로고    scopus 로고
    • Compensation for spin-spin coupling effects during adiabatic pulses
    • E. Kupce, and R. Freeman Compensation for spin-spin coupling effects during adiabatic pulses J. Magn. Reson. 127 1997 36 48
    • (1997) J. Magn. Reson. , vol.127 , pp. 36-48
    • Kupce, E.1    Freeman, R.2
  • 40
    • 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 1992 10663 10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3


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