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Volumn 49, Issue 1, 2011, Pages 53-60

Residual dipolar couplings: Are multiple independent alignments always possible?

Author keywords

Dynamics; Hen egg white lysozyme; Protein alignment; Residual dipolar couplings; Ubiquitin

Indexed keywords

HEN EGG WHITE LYSOZYME; HIGH MOBILITY GROUP B1 PROTEIN; HIGH MOBILITY GROUP B3 PROTEIN; LYSOZYME; POLYACRYLAMIDE GEL; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 79951552152     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-010-9457-1     Document Type: Article
Times cited : (28)

References (45)
  • 1
    • 0034066681 scopus 로고    scopus 로고
    • Characterization of surfactant liquid crystal phases suitable for molecular alignment and measurement of dipolar couplings
    • DOI 10.1023/A:1008356618658
    • LG Barrientos C Dolan AM Gronenborn 2000 Characterization of surfactant liquid crystal phases suitable for molecular alignment and measurement of dipolar couplings J Biomol NMR 16 329 337 10.1023/A:1008356618658 (Pubitemid 30262562)
    • (2000) Journal of Biomolecular NMR , vol.16 , Issue.4 , pp. 329-337
    • Barrientos, L.G.1    Dolan, C.2    Gronenborn, A.M.3
  • 3
    • 1842862935 scopus 로고    scopus 로고
    • Anisotropic Small Amplitude Peptide Plane Dynamics in Proteins from Residual Dipolar Couplings
    • DOI 10.1021/ja036977w
    • P Bernadó M Blackledge 2004 Anisotropic small amplitude peptide plane dynamics in proteins from residual dipolar couplings J Am Chem Soc 126 4907 4920 10.1021/ja036977w (Pubitemid 38490158)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.15 , pp. 4907-4920
    • Bernado, P.1    Blackledge, M.2
  • 4
    • 3042588804 scopus 로고    scopus 로고
    • Local dynamic amplitudes on the protein backbone from dipolar couplings: Toward the elucidation of slower motions in biomolecules
    • DOI 10.1021/ja048785m
    • P Bernadó M Blackledge 2004 Local dynamic amplitude on the protein backbone from dipolar couplings: toward the elucidation of slower motions in biomolecules J Am Chem Soc 126 7760 7761 10.1021/ja048785m (Pubitemid 38812751)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.25 , pp. 7760-7761
    • Bernado, P.1    Blackledge, M.2
  • 5
    • 33845203743 scopus 로고    scopus 로고
    • Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings
    • DOI 10.1021/ja066704b
    • G Bouvignies P Markwick R Brüschweiler M Blackledge 2006 Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings J Am Chem Soc 128 15100 15101 10.1021/ja066704b (Pubitemid 44853519)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.47 , pp. 15100-15101
    • Bouvignies, G.1    Markwick, P.2    Bruschweiler, R.3    Blackledge, M.4
  • 6
    • 0032560968 scopus 로고    scopus 로고
    • 15N NMR relaxation data for a protein in solution [7]
    • DOI 10.1021/ja9815733
    • 15N NMR relaxation data for a protein in solution J Am Chem Soc 120 9692 9693 10.1021/ja9815733 (Pubitemid 28452667)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.37 , pp. 9692-9693
    • Boyd, J.1    Redfield, C.2
  • 7
    • 0033581191 scopus 로고    scopus 로고
    • 15N chemical shifts in dilute bicelle solutions [19]
    • DOI 10.1021/ja9911216
    • 15N chemical shifts in dilute bicelle solutions J Am Chem Soc 121 7441 7442 10.1021/ja9911216 (Pubitemid 29400184)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.32 , pp. 7441-7442
    • Boyd, J.1    Redfield, C.2
  • 9
    • 0032705883 scopus 로고    scopus 로고
    • Internal and overall peptide group motion in proteins: Molecular dynamics simulations for lysozyme compared with results from X-ray and NMR spectroscopy
    • DOI 10.1021/ja991309p
    • M Buck M Karplus 1999 Internal and overall peptide group motion in proteins: molecular dynamics simulations for lysozyme compared with results from X-ray and NMR spectroscopy J Am Chem Soc 121 9645 9658 10.1021/ja991309p (Pubitemid 29498488)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.41 , pp. 9645-9658
    • Buck, M.1    Karplus, M.2
  • 11
    • 4143079167 scopus 로고    scopus 로고
    • Amplitudes of protein backbone dynamics and correlated motions in a small α/β protein: Correspondence of dipolar coupling and heteronuclear relaxation measurements
    • DOI 10.1021/bi049357w
    • GM Clore CD Schwieters 2004 Amplitudes of protein backbone dynamics and correlated motions in a small alpha/beta protein: correspondence of dipolar coupling and heteronuclear relaxation measurements Biochemistry 43 10678 10691 10.1021/bi049357w (Pubitemid 39096710)
    • (2004) Biochemistry , vol.43 , Issue.33 , pp. 10678-10691
    • Clore, G.M.1    Schwieters, C.D.2
  • 12
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • DOI 10.1021/ja9812610
    • G Cornilescu JL Marquardt M Ottiger A Bax 1998 Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase J Am Chem Soc 120 6836 6837 10.1021/ja9812610 (Pubitemid 28347351)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.27 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 13
    • 10444250148 scopus 로고    scopus 로고
    • Residual dipolar couplings and some specific models for motional averaging
    • 10.1016/j.jmr.2004.09.023 2005JMagR.172.118D
    • M Deschamps ID Campbell J Boyd 2005 Residual dipolar couplings and some specific models for motional averaging J Magn Res 172 118 132 10.1016/j.jmr.2004.09.023 2005JMagR.172..118D
    • (2005) J Magn Res , vol.172 , pp. 118-132
    • Deschamps, M.1    Campbell, I.D.2    Boyd, J.3
  • 15
    • 11344264678 scopus 로고    scopus 로고
    • Asparagine and glutamine side-chain conformation in solution and crystal: A comparison for hen egg-white lysozyme using residual dipolar couplings
    • DOI 10.1007/s10858-004-3218-y
    • VA Higman J Boyd LJ Smith C Redfield 2004 Asparagine and glutamine side-chain conformations in solution and crystal: a comparison for hen egg-white lysozyme using residual dipolar couplings J Biomol NMR 30 327 346 10.1007/s10858-004-3218-y (Pubitemid 40073583)
    • (2004) Journal of Biomolecular NMR , vol.30 , Issue.3 , pp. 327-346
    • Higman, V.A.1    Boyd, J.2    Smith, L.J.3    Redfield, C.4
  • 16
    • 0036813901 scopus 로고    scopus 로고
    • Principal component method for assessing structural heterogeneity across multiple alignment media
    • DOI 10.1023/A:1020927930910
    • J-C Hus R Brüschweiler 2002 Principal component method for assessing structural heterogeneity across multiple alignment media J Biomol NMR 24 123 132 10.1023/A:1020927930910 (Pubitemid 35414675)
    • (2002) Journal of Biomolecular NMR , vol.24 , Issue.2 , pp. 123-132
    • Hus, J.-C.1    Bruschweiler, R.2
  • 17
    • 0037508925 scopus 로고    scopus 로고
    • Self-consistency analysis of dipolar couplings in multiple alignments of ubiquitin
    • DOI 10.1021/ja029719s
    • J-C Hus W Peti C Griesinger R Brüschweiler 2003 Self-consistency analysis of dipolar couplings in multiple alignments of ubiquitin J Am Chem Soc 125 5596 5597 10.1021/ja029719s (Pubitemid 36592859)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.19 , pp. 5596-5597
    • Hus, J.-C.1    Peti, W.2    Griesinger, C.3    Bruschweiler, R.4
  • 18
    • 33645469988 scopus 로고    scopus 로고
    • A thorough dynamic interpretation of residual dipolar couplings in ubiquitin
    • 10.1007/s10858-005-5686-0
    • NA Lakomek T Carlomagno S Becker C Griesinger J Meiler 2006 A thorough dynamic interpretation of residual dipolar couplings in ubiquitin J Biomol NMR 34 101 115 10.1007/s10858-005-5686-0
    • (2006) J Biomol NMR , vol.34 , pp. 101-115
    • Lakomek, N.A.1    Carlomagno, T.2    Becker, S.3    Griesinger, C.4    Meiler, J.5
  • 20
    • 38349001213 scopus 로고    scopus 로고
    • Comparison of alignment tensors generated for native tRNA(Val) using magnetic fields and liquid crystalline media
    • 10.1007/s10858-007-9212-4
    • MP Latham P Hanson DJ Brown A Pardi 2008 Comparison of alignment tensors generated for native tRNA(Val) using magnetic fields and liquid crystalline media J Biomol NMR 40 83 94 10.1007/s10858-007-9212-4
    • (2008) J Biomol NMR , vol.40 , pp. 83-94
    • Latham, M.P.1    Hanson, P.2    Brown, D.J.3    Pardi, A.4
  • 21
    • 0034820148 scopus 로고    scopus 로고
    • Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins
    • DOI 10.1021/ja010002z
    • J Meiler JJ Prompers W Peti C Griesinger R Brüschweiler 2001 Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins J Am Chem Soc 123 6098 6107 10.1021/ja010002z (Pubitemid 32888479)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.25 , pp. 6098-6107
    • Meiler, J.1    Prompers, J.J.2    Peti, W.3    Griesinger, C.4    Bruschweiler, R.5
  • 22
    • 0002473875 scopus 로고    scopus 로고
    • HH Coupling Constants
    • A Meissner J∅ Duus OW Sørensen 1997 Spin-state-selective excitation. Application for E.COSY-type measurement of JHH coupling constants J Magn Res 128 92 97 10.1006/jmre.1997.1213 1997JMagR.128...92M (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
  • 23
    • 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 Res 131 373 378 10.1006/jmre.1998.1361 1998JMagR.131..373O (Pubitemid 128450579)
    • (1998) Journal of Magnetic Resonance , vol.131 , Issue.2 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 24
    • 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 Brüschweiler 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
  • 25
    • 0032500340 scopus 로고    scopus 로고
    • Modulation of the alignment tensor of macromolecules dissolved in a dilute liquid crystalline medium [19]
    • DOI 10.1021/ja982310b
    • BE Ramirez A Bax 1998 Modulation of the alignment tensor of macromolecules dissolved in a dilute liquid crystalline medium J Am Chem Soc 120 9106 9107 10.1021/ja982310b (Pubitemid 28449207)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.35 , pp. 9106-9107
    • Ramirez, B.E.1    Bax, A.2
  • 26
    • 27544456324 scopus 로고    scopus 로고
    • Composite alignment media for the measurement of independent sets of NMR residual dipolar couplings
    • DOI 10.1021/ja055520e
    • K Ruan JR Tolman 2005 Composite alignment media for the measurement of independent sets of NMR residual dipolar couplings J Am Chem Soc 127 15032 15033 10.1021/ja055520e (Pubitemid 41547363)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.43 , pp. 15032-15033
    • Ruan, K.1    Tolman, J.R.2
  • 27
    • 44949209342 scopus 로고    scopus 로고
    • De novo determination of internuclear vector orientations from residual dipolar couplings measured in three independent alignment media
    • 10.1007/s10858-008-9240-8
    • K Ruan KB Briggman JR Tolman 2008 De novo determination of internuclear vector orientations from residual dipolar couplings measured in three independent alignment media J Biomol NMR 41 61 76 10.1007/s10858-008-9240-8
    • (2008) J Biomol NMR , vol.41 , pp. 61-76
    • Ruan, K.1    Briggman, K.B.2    Tolman, J.R.3
  • 28
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • 10.1021/ja001068h
    • M Rückert G Otting 2000 Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments J Am Chem Soc 122 7793 7797 10.1021/ja001068h
    • (2000) J Am Chem Soc , vol.122 , pp. 7793-7797
    • Rückert, M.1    Otting, G.2
  • 30
    • 0034501042 scopus 로고    scopus 로고
    • Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes
    • DOI 10.1023/A:1026703605147
    • H-J Sass G Musco SJ Stahl PT Wingfield S Grzesiek 2000 Solution NMR of proteins within polyacrylamide gels: diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes J Biomol NMR 18 303 309 10.1023/A:1026703605147 (Pubitemid 32065084)
    • (2000) Journal of Biomolecular NMR , vol.18 , Issue.4 , pp. 303-309
    • Sass, H.-J.1    Musco, G.2    J. Stahl, S.3    T. Wingfield, P.4    Grzesiek, S.5
  • 32
    • 0029162947 scopus 로고
    • Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changes
    • 10.1021/bi00034a026
    • LJ Smith AE Mark CM Dobson WF van Gunsteren 1995 Comparison of MD simulations and NMR experiments for hen lysozyme. Analysis of local fluctuations, cooperative motions, and global changes Biochemistry 34 10918 10931 10.1021/bi00034a026
    • (1995) Biochemistry , vol.34 , pp. 10918-10931
    • Smith, L.J.1    Mark, A.E.2    Dobson, C.M.3    Van Gunsteren, W.F.4
  • 33
    • 11244289541 scopus 로고    scopus 로고
    • Validation of the GROMOS force-field parameter set 45A3 against nuclear magnetic resonance data of hen egg lysozyme
    • DOI 10.1007/s10858-004-5430-1
    • TA Soares X Daura C Oostenbrink LJ Smith WF van Gunsteren 2004 Validation of the GROMOS force-field parameter set 45A3 against nuclear magnetic resonance data of hen egg lysozyme J Biomol NMR 30 407 422 10.1007/s10858-004-5430-1 (Pubitemid 40069205)
    • (2004) Journal of Biomolecular NMR , vol.30 , Issue.4 , pp. 407-422
    • Soares, T.A.1    Daura, X.2    Oostenbrink, C.3    Smith, L.J.4    Van Gunsteren, W.F.5
  • 35
    • 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
  • 36
    • 67649523535 scopus 로고    scopus 로고
    • Protein dynamics from disorder
    • 10.1038/4591063a 2009Natur.459.1063T
    • JR Tolman 2009 Protein dynamics from disorder Nature 459 1063 1064 10.1038/4591063a 2009Natur.459.1063T
    • (2009) Nature , vol.459 , pp. 1063-1064
    • Tolman, J.R.1
  • 37
  • 38
    • 0042367594 scopus 로고    scopus 로고
    • Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy
    • DOI 10.1021/ja0350684
    • TS Ulmer BE Ramirez F Delaglio A Bax 2003 Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy J Am Chem Soc 125 9179 9191 10.1021/ja0350684 (Pubitemid 36903834)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.30 , pp. 9179-9191
    • Ulmer, T.S.1    Ramirez, B.E.2    Delaglio, F.3    Bax, A.4
  • 39
    • 0000695363 scopus 로고    scopus 로고
    • High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from spaceHab-01 mission
    • MC Vaney S Maignan M Riès-Kautt A Ducruix 1996 High-resolution structure (1.33 Å) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission Acta Crystallogr D 52 505 517 10.1107/S090744499501674X (Pubitemid 126516233)
    • (1996) Acta Crystallographica Section D: Biological Crystallography , vol.52 , Issue.3 , pp. 505-517
    • Vaney, M.C.1    Maignan, S.2    Ries-Kautt, M.3    Ducruix, A.4
  • 40
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • 10.1016/0022-2836(87)90679-6
    • S Vijay-Kumar CE Bugg WJ Cook 1987 Structure of ubiquitin refined at 1.8 Å resolution J Mol Biol 194 531 544 10.1016/0022-2836(87)90679-6
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 42
    • 0242299265 scopus 로고    scopus 로고
    • Protein Alignment by a Coexpressed Lanthanide-Binding Tag for the Measurement of Residual Dipolar Couplings
    • DOI 10.1021/ja036022d
    • J Wöhnert KJ Franz M Nitz B Imperiali H Schwalbe 2003 Protein alignment by coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings J Am Chem Soc 125 13338 13339 10.1021/ja036022d (Pubitemid 37352103)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.44 , pp. 13338-13339
    • Wohnert, J.1    Franz, K.J.2    Nitz, M.3    Imperiali, B.4    Schwalbe, H.5
  • 43
    • 35048901140 scopus 로고    scopus 로고
    • Modulating protein alignment in a liquid-crystalline medium through conservative mutagenesis
    • DOI 10.1021/ja073937+
    • L Yao A Bax 2007 Modulating protein alignment in a liquid-crystalline medium through conservative mutagenesis J Am Chem Soc 129 11326 11327 10.1021/ja073937+ (Pubitemid 47555539)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.37 , pp. 11326-11327
    • Yao, L.1    Bax, A.2
  • 44
    • 44949168516 scopus 로고    scopus 로고
    • Simultaneous NMR study of protein structure and dynamics using conservative mutagenesis
    • 10.1021/jp0772124
    • L Yao B Vögeli 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    Vögeli, B.2    Torchia, D.A.3    Bax, A.4
  • 45
    • 0035996721 scopus 로고    scopus 로고
    • Evaluation of uncertainty in alignment tensors obtained from dipolar couplings
    • DOI 10.1023/A:1016316415261
    • M Zweckstetter A Bax 2002 Evaluation of uncertainty in alignment tensors obtained from dipolar couplings J Biomol NMR 23 127 137 10.1023/A:1016316415261 (Pubitemid 34778165)
    • (2002) Journal of Biomolecular NMR , vol.23 , Issue.2 , pp. 127-137
    • Zweckstetter, M.1    Bax, A.2


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