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Volumn 40, Issue 12, 2011, Pages 1371-1381

Characterizing weak protein-protein complexes by NMR residual dipolar couplings

Author keywords

Complex; Dynamics; Interaction; NMR; Protein; Structure

Indexed keywords

PROTEIN;

EID: 82455187977     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-011-0720-5     Document Type: Article
Times cited : (13)

References (57)
  • 1
    • 74849106907 scopus 로고    scopus 로고
    • Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase
    • 19961227 10.1021/ja9064574 1:CAS:528:DC%2BD1MXhsFWmurrI
    • Q Bashir, et al. 2010 Visualization of the encounter ensemble of the transient electron transfer complex of cytochrome c and cytochrome c peroxidase J Am Chem Soc 132 241 247 19961227 10.1021/ja9064574 1:CAS:528: DC%2BD1MXhsFWmurrI
    • (2010) J Am Chem Soc , vol.132 , pp. 241-247
    • Bashir, Q.1
  • 2
    • 0037215324 scopus 로고    scopus 로고
    • Weak alignment offers new NMR opportunities to study protein structure and dynamics
    • DOI 10.1110/ps.0233303
    • A Bax 2003 Weak alignment offers new NMR opportunities to study protein structure and dynamics Protein Sci 12 1 16 12493823 10.1110/ps.0233303 1:CAS:528:DC%2BD3sXht1ehuw%3D%3D (Pubitemid 36020129)
    • (2003) Protein Science , vol.12 , Issue.1 , pp. 1-16
    • Bax, A.1
  • 3
    • 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 16140525 10.1016/j.sbi.2005.08.006 1:CAS:528:DC%2BD2MXhtVKjsLzJ (Pubitemid 41393488)
    • (2005) Current Opinion in Structural Biology , vol.15 , Issue.5 , pp. 563-570
    • Bax, A.1    Grishaev, A.2
  • 4
    • 67650539779 scopus 로고    scopus 로고
    • Simultaneous measurement of residual dipolar couplings for proteins in complex using the isotopically discriminated NMR approach
    • 19485366 10.1021/ja901602c 1:CAS:528:DC%2BD1MXms1egu7g%3D
    • W Bermel, et al. 2009 Simultaneous measurement of residual dipolar couplings for proteins in complex using the isotopically discriminated NMR approach J Am Chem Soc 131 8564 8570 19485366 10.1021/ja901602c 1:CAS:528:DC%2BD1MXms1egu7g%3D
    • (2009) J Am Chem Soc , vol.131 , pp. 8564-8570
    • Bermel, W.1
  • 5
    • 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 amplitudes on the protein backbone from dipolar couplings: toward the elucidation of slower motions in biomolecules J Am Chem Soc 126 7760 7761 15212507 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
  • 6
    • 50149104140 scopus 로고    scopus 로고
    • Interactions between the three CIN85 SH3 domains and ubiquitin: Implications for CIN85 ubiquitination
    • 18680311 10.1021/bi800439t 1:CAS:528:DC%2BD1cXptlejs7Y%3D
    • I Bezsonova, et al. 2008 Interactions between the three CIN85 SH3 domains and ubiquitin: implications for CIN85 ubiquitination Biochemistry 47 8937 8949 18680311 10.1021/bi800439t 1:CAS:528:DC%2BD1cXptlejs7Y%3D
    • (2008) Biochemistry , vol.47 , pp. 8937-8949
    • Bezsonova, I.1
  • 7
    • 14844353335 scopus 로고    scopus 로고
    • Recent progress in the study of biomolecular structure and dynamics in solution from residual dipolar couplings
    • DOI 10.1016/j.pnmrs.2004.11.002, PII S0079656504000603
    • M Blackledge 2005 Recent progress in the study of biomolecular structure and dynamics in solution from residual dipolar couplings Prog Nucl Magn Reson Spectrosc 46 23 61 10.1016/j.pnmrs.2004.11.002 1:CAS:528:DC%2BD2MXisFahtrY%3D (Pubitemid 40357061)
    • (2005) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.46 , Issue.1 , pp. 23-61
    • Blackledge, M.1
  • 8
    • 0033569503 scopus 로고    scopus 로고
    • Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complex
    • DOI 10.1006/jmbi.1999.3133
    • PJ Bolon HM Al-Hashimi JH Prestegard 1999 Residual dipolar coupling derived orientational constraints on ligand geometry in a 53 kDa protein-ligand complex J Mol Biol 293 107 115 10512719 10.1006/jmbi.1999.3133 1:CAS:528:DyaK1MXmtlCrsb0%3D (Pubitemid 29494873)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.1 , pp. 107-115
    • Bolon, P.J.1    Al-Hashimi, H.M.2    Prestegard, J.H.3
  • 10
    • 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 17117856 10.1021/ja066704b 1:CAS:528:DC%2BD28XhtFKrs7bL (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
  • 11
    • 1542317796 scopus 로고    scopus 로고
    • How Much Backbone Motion in Ubiquitin Is Required to Account for Dipolar Coupling Data Measured in Multiple Alignment Media as Assessed by Independent Cross-Validation?
    • DOI 10.1021/ja0386804
    • GM Clore CD Schwieters 2004 How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation? J Am Chem Soc 126 2923 2938 14995210 10.1021/ja0386804 1:CAS:528:DC%2BD2cXhtFagtrg%3D (Pubitemid 38314298)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.9 , pp. 2923-2938
    • Clore, G.M.1    Schwieters, C.D.2
  • 12
    • 0032517327 scopus 로고    scopus 로고
    • Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses [15]
    • DOI 10.1021/ja982592f
    • GM Clore MR Starich AM Gronenborn 1998 Measurement of residual dipolar couplings of macromolecules aligned in the nematic phase of a colloidal suspension of rod-shaped viruses J Am Chem Soc 120 10571 10572 10.1021/ja982592f 1:CAS:528:DyaK1cXmtV2ltbs%3D (Pubitemid 28500376)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.40 , pp. 10571-10572
    • Clore, G.M.1    Starich, M.R.2    Gronenborn, A.M.3
  • 13
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • DOI 10.1021/ja026939x
    • C Dominguez R Boelens AMJJ Bonvin 2003 HADDOCK: a protein-protein docking approach based on biochemical or biophysical information J Am Chem Soc 125 1731 1737 12580598 10.1021/ja026939x 1:CAS:528:DC%2BD3sXkvFGquw%3D%3D (Pubitemid 36232568)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.7 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 15
    • 35948942349 scopus 로고    scopus 로고
    • NMR methods for the determination of protein-ligand dissociation constants
    • DOI 10.1016/j.pnmrs.2007.04.001, PII S0079656507000258
    • L Fielding 2007 NMR methods for the determination of protein-ligand dissociation constants Prog Nucl Magn Reson Spectrosc 51 219 242 10.1016/j.pnmrs.2007.04.001 1:CAS:528:DC%2BD2sXht1ynu77I (Pubitemid 350064300)
    • (2007) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.51 , Issue.4 , pp. 219-242
    • Fielding, L.1
  • 16
    • 0031760503 scopus 로고    scopus 로고
    • Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions
    • DOI 10.1038/4176
    • MR Hansen L Mueller A Pardi 1998 Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions Nat Struct Biol 5 1065 1074 9846877 10.1038/4176 1:CAS:528:DyaK1cXnvFOlu7k%3D (Pubitemid 28546270)
    • (1998) Nature Structural Biology , vol.5 , Issue.12 , pp. 1065-1074
    • Hansen, M.R.1    Mueller, L.2    Pardi, A.3
  • 17
    • 34548564106 scopus 로고    scopus 로고
    • Structural Basis for Ubiquitin Recognition by SH3 Domains
    • DOI 10.1016/j.jmb.2007.07.074, PII S0022283607010522
    • Y He L Hicke I Radhakrishnan 2007 Structural basis for ubiquitin recognition by SH3 domains J Mol Biol 373 190 196 17765920 10.1016/j.jmb.2007. 07.074 1:CAS:528:DC%2BD2sXhtVCgtbbO (Pubitemid 47390722)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.1 , pp. 190-196
    • He, Y.1    Hicke, L.2    Radhakrishnan, I.3
  • 18
    • 56749158755 scopus 로고    scopus 로고
    • 16-fold degeneracy of peptide plane orientations from residual dipolar couplings: Analytical treatment and implications for protein structure determination
    • 18959402 10.1021/ja804274s 1:CAS:528:DC%2BD1cXhtlWqurjK
    • J Hus, et al. 2008 16-fold degeneracy of peptide plane orientations from residual dipolar couplings: analytical treatment and implications for protein structure determination J Am Chem Soc 130 15927 15937 18959402 10.1021/ja804274s 1:CAS:528:DC%2BD1cXhtlWqurjK
    • (2008) J Am Chem Soc , vol.130 , pp. 15927-15937
    • Hus, J.1
  • 19
    • 0037466291 scopus 로고    scopus 로고
    • Structural characterization of a mannose-binding protein - Trimannoside complex using residual dipolar couplings
    • DOI 10.1016/S0022-2836(03)00268-7
    • NU Jain S Noble JH Prestegard 2003 Structural characterization of a mannose-binding protein-trimannoside complex using residual dipolar couplings J Mol Biol 328 451 462 12691753 10.1016/S0022-2836(03)00268-7 1:CAS:528: DC%2BD3sXisleht78%3D (Pubitemid 36407587)
    • (2003) Journal of Molecular Biology , vol.328 , Issue.2 , pp. 451-462
    • Jain, N.U.1    Noble, S.2    Prestegard, J.H.3
  • 20
    • 6344231261 scopus 로고    scopus 로고
    • Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: The 95 kDa complex of LpxA with acyl carrier protein
    • DOI 10.1016/j.jmb.2004.08.103, PII S0022283604011143
    • NU Jain, et al. 2004 Rapid analysis of large protein-protein complexes using NMR-derived orientational constraints: the 95 kDa complex of LpxA with acyl carrier protein J Mol Biol 343 1379 1389 15491619 10.1016/j.jmb.2004.08.103 1:CAS:528:DC%2BD2cXos1Kksr4%3D (Pubitemid 39387832)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.5 , pp. 1379-1389
    • Jain, N.U.1    Wyckoff, T.J.O.2    Raetz, C.R.H.3    Prestegard, J.H.4
  • 21
    • 45749102885 scopus 로고    scopus 로고
    • Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: Application to the molecular recognition element of Sendai virus nucleoprotein
    • DOI 10.1021/ja801332d
    • MR Jensen, et al. 2008 Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: application to the molecular recognition element of Sendai virus nucleoprotein J Am Chem Soc 130 8055 8061 18507376 10.1021/ja801332d 1:CAS:528:DC%2BD1cXmsVelsbg%3D (Pubitemid 351875082)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.25 , pp. 8055-8061
    • Jensen, M.R.1    Houben, K.2    Lescop, E.3    Blanchard, L.4    Ruigrok, R.W.H.5    Blackledge, M.6
  • 22
    • 69849103777 scopus 로고    scopus 로고
    • Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings
    • 19748338 10.1016/j.str.2009.08.001 1:CAS:528:DC%2BD1MXhtFanu7jN
    • MR Jensen, et al. 2009 Quantitative determination of the conformational properties of partially folded and intrinsically disordered proteins using NMR dipolar couplings Structure 17 1169 1185 19748338 10.1016/j.str.2009.08.001 1:CAS:528:DC%2BD1MXhtFanu7jN
    • (2009) Structure , vol.17 , pp. 1169-1185
    • Jensen, M.R.1
  • 23
    • 53149091683 scopus 로고    scopus 로고
    • Distinct interactions between ubiquitin and the SH3 domains involved in immune signaling
    • 18539162 1:CAS:528:DC%2BD1cXhtVShs73I
    • J Kang, et al. 2008 Distinct interactions between ubiquitin and the SH3 domains involved in immune signaling Biochim Biophys Acta 1784 1335 1341 18539162 1:CAS:528:DC%2BD1cXhtVShs73I
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1335-1341
    • Kang, J.1
  • 24
    • 0036385914 scopus 로고    scopus 로고
    • Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings
    • 12217702 10.1016/S0022-2836(02)00745-3 1:CAS:528:DC%2BD38Xms1Wru7o%3D
    • BW Koenig, et al. 2002 Structure and orientation of a G protein fragment in the receptor bound state from residual dipolar couplings J Mol Biol 322 441 461 12217702 10.1016/S0022-2836(02)00745-3 1:CAS:528:DC%2BD38Xms1Wru7o%3D
    • (2002) J Mol Biol , vol.322 , pp. 441-461
    • Koenig, B.W.1
  • 25
    • 59149097809 scopus 로고    scopus 로고
    • Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy
    • 19111555 10.1016/j.jmb.2008.11.055 1:CAS:528:DC%2BD1MXhs1arsrY%3D
    • DM Korzhnev, et al. 2009 Alternate binding modes for a ubiquitin-SH3 domain interaction studied by NMR spectroscopy J Mol Biol 386 391 405 19111555 10.1016/j.jmb.2008.11.055 1:CAS:528:DC%2BD1MXhs1arsrY%3D
    • (2009) J Mol Biol , vol.386 , pp. 391-405
    • Korzhnev, D.M.1
  • 27
    • 78650907948 scopus 로고    scopus 로고
    • NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin
    • 10.1021/bi101594a
    • A Lange, et al. 2010 NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin Biochemistry 50 48 62 10.1021/bi101594a
    • (2010) Biochemistry , vol.50 , pp. 48-62
    • Lange, A.1
  • 28
    • 77956361185 scopus 로고    scopus 로고
    • Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping
    • 20589905 10.1002/pro.447 1:CAS:528:DC%2BC3cXhtV2gsLrO
    • H Lee, et al. 2010 Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping Protein Sci 19 1673 1685 20589905 10.1002/pro.447 1:CAS:528:DC%2BC3cXhtV2gsLrO
    • (2010) Protein Sci , vol.19 , pp. 1673-1685
    • Lee, H.1
  • 29
    • 3042691762 scopus 로고    scopus 로고
    • Residual dipolar couplings in NMR structure analysis
    • DOI 10.1146/annurev.biophys.33.110502.140306
    • RS Lipsitz N Tjandra 2004 Residual dipolar couplings in NMR structure analysis Annu Rev Biophys Biomol Struct 33 387 413 15139819 10.1146/annurev. biophys.33.110502.140306 1:CAS:528:DC%2BD2cXltlKkt7g%3D (Pubitemid 38829965)
    • (2004) Annual Review of Biophysics and Biomolecular Structure , vol.33 , pp. 387-413
    • Lipsitz, R.S.1    Tjandra, N.2
  • 30
    • 70450237199 scopus 로고    scopus 로고
    • Toward a unified representation of protein structural dynamics in solution
    • 19919148 10.1021/ja907476w 1:CAS:528:DC%2BD1MXhtlGjtrzF
    • PRL Markwick, et al. 2009 Toward a unified representation of protein structural dynamics in solution J Am Chem Soc 131 16968 16975 19919148 10.1021/ja907476w 1:CAS:528:DC%2BD1MXhtlGjtrzF
    • (2009) J Am Chem Soc , vol.131 , pp. 16968-16975
    • Markwick, P.R.L.1
  • 31
    • 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, et al. 2001 Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins J Am Chem Soc 123 6098 6107 11414844 10.1021/ja010002z 1:CAS:528:DC%2BD3MXjvVWhsr0%3D (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
  • 32
    • 71749087100 scopus 로고    scopus 로고
    • Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings
    • 19908838 10.1021/ja9069024 1:CAS:528:DC%2BD1MXhsVSmu7zK
    • G Nodet L Salmon V Ozenne S Meier MR Jensen M Blackledge 2009 Quantitative description of backbone conformational sampling of unfolded proteins at amino acid resolution from NMR residual dipolar couplings J Am Chem Soc 131 17908 17918 19908838 10.1021/ja9069024 1:CAS:528:DC%2BD1MXhsVSmu7zK
    • (2009) J Am Chem Soc , vol.131 , pp. 17908-17918
    • Nodet, G.1    Salmon, L.2    Ozenne, V.3    Meier, S.4    Jensen, M.R.5    Blackledge, M.6
  • 33
    • 73249139292 scopus 로고    scopus 로고
    • The structural analysis of protein-protein interactions by NMR spectroscopy
    • 19834907 10.1002/pmic.200900303
    • MR O'Connell R Gamsjaeger JP Mackay 2009 The structural analysis of protein-protein interactions by NMR spectroscopy Proteomics 9 5224 5232 19834907 10.1002/pmic.200900303
    • (2009) Proteomics , vol.9 , pp. 5224-5232
    • O'Connell, M.R.1    Gamsjaeger, R.2    MacKay, J.P.3
  • 35
    • 66249142325 scopus 로고    scopus 로고
    • Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: Application to the CD2AP SH3-C:ubiquitin complex
    • 19359362 10.1093/nar/gkp211
    • JL Ortega Roldan, et al. 2009 Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex Nucleic Acids Res 37 e70 19359362 10.1093/nar/gkp211
    • (2009) Nucleic Acids Res , vol.37 , pp. 70
    • Ortega Roldan, J.L.1
  • 36
    • 80051688323 scopus 로고    scopus 로고
    • Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP
    • Ortega Roldan JL, Blackledge M, van Nuland NAJ, Azuaga AI (2011) Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP. J Biomol NMR 50:103-117
    • (2011) J Biomol NMR , vol.50 , pp. 103-117
    • Ortega Roldan, J.L.1    Blackledge, M.2    Van Nuland Naj3    Azuaga, A.I.4
  • 37
    • 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 11233409 10.1017/S0033583500003656 1:CAS:528:DC%2BD3MXntFGmurg%3D (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
  • 38
    • 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
  • 39
    • 70349784868 scopus 로고    scopus 로고
    • Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: Quantitative and absolute determination of backbone motion in ubiquitin
    • 10.1002/anie.200900476 1:CAS:528:DC%2BD1MXmsVSit74%3D
    • L Salmon, et al. 2009 Protein conformational flexibility from structure-free analysis of NMR dipolar couplings: quantitative and absolute determination of backbone motion in ubiquitin Angew Chem 48 4154 4157 10.1002/anie.200900476 1:CAS:528:DC%2BD1MXmsVSit74%3D
    • (2009) Angew Chem , vol.48 , pp. 4154-4157
    • Salmon, L.1
  • 40
    • 77953627413 scopus 로고    scopus 로고
    • NMR characterization of long-range order in intrinsically disordered proteins
    • 20499903 10.1021/ja101645g 1:CAS:528:DC%2BC3cXmsFOks74%3D
    • L Salmon, et al. 2010 NMR characterization of long-range order in intrinsically disordered proteins J Am Chem Soc 132 8407 8418 20499903 10.1021/ja101645g 1:CAS:528:DC%2BC3cXmsFOks74%3D
    • (2010) J Am Chem Soc , vol.132 , pp. 8407-8418
    • Salmon, L.1
  • 41
    • 79953699641 scopus 로고    scopus 로고
    • Structure, dynamics, and kinetics of weak protein-protein complexes from NMR spin relaxation measurements of titrated solutions
    • 10.1002/anie.201100310 1:CAS:528:DC%2BC3MXkt12jur4%3D
    • L Salmon, et al. 2011 Structure, dynamics, and kinetics of weak protein-protein complexes from NMR spin relaxation measurements of titrated solutions Angew Chem 50 3755 3759 10.1002/anie.201100310 1:CAS:528: DC%2BC3MXkt12jur4%3D
    • (2011) Angew Chem , vol.50 , pp. 3755-3759
    • Salmon, L.1
  • 42
    • 79953718077 scopus 로고    scopus 로고
    • Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scales
    • 21388216 10.1021/bi200177v 1:CAS:528:DC%2BC3MXjsVygt7g%3D
    • L Salmon G Bouvignies P Markwick M Blackledge 2011 Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scales Biochemistry 50 2735 2747 21388216 10.1021/bi200177v 1:CAS:528:DC%2BC3MXjsVygt7g%3D
    • (2011) Biochemistry , vol.50 , pp. 2735-2747
    • Salmon, L.1    Bouvignies, G.2    Markwick, P.3    Blackledge, M.4
  • 43
    • 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
    • HJ Sass, et al. 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 11200524 10.1023/A:1026703605147 1:CAS:528:DC%2BD3MXns1KisQ%3D%3D (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
  • 44
    • 79551681222 scopus 로고    scopus 로고
    • Protein binding specificity versus promiscuity
    • 21071205 10.1016/j.sbi.2010.10.002 1:CAS:528:DC%2BC3MXhvFKhur0%3D
    • G Schreiber AE Keating 2011 Protein binding specificity versus promiscuity Curr Opin Struct Biol 21 50 61 21071205 10.1016/j.sbi.2010.10.002 1:CAS:528:DC%2BC3MXhvFKhur0%3D
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 50-61
    • Schreiber, G.1    Keating, A.E.2
  • 45
    • 33846212272 scopus 로고    scopus 로고
    • Ubiquitin Binds to and Regulates a Subset of SH3 Domains
    • DOI 10.1016/j.molcel.2006.12.016, PII S1097276506008847
    • SD Stamenova, et al. 2007 Ubiquitin binds to and regulates a subset of SH3 domains Mol Cell 25 273 284 17244534 10.1016/j.molcel.2006.12.016 1:CAS:528:DC%2BD2sXhslKju7w%3D (Pubitemid 46109609)
    • (2007) Molecular Cell , vol.25 , Issue.2 , pp. 273-284
    • Stamenova, S.D.1    French, M.E.2    He, Y.3    Francis, S.A.4    Kramer, Z.B.5    Hicke, L.6
  • 46
    • 32344445231 scopus 로고    scopus 로고
    • NMR studies of protein interactions
    • DOI 10.1016/j.sbi.2006.01.006, PII S0959440X0600011X
    • K Takeuchi G Wagner 2006 NMR studies of protein interactions Curr Opin Struct Biol 16 109 117 16427776 10.1016/j.sbi.2006.01.006 1:CAS:528: DC%2BD28XhsFOjsrg%3D (Pubitemid 43221879)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.1 , pp. 109-117
    • Takeuchi, K.1    Wagner, G.2
  • 47
    • 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 9353189 10.1126/science.278.5340.1111 1:CAS:528:DyaK2sXnt1aju7c%3D (Pubitemid 27517889)
    • (1997) Science , vol.278 , Issue.5340 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 48
    • 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
    • 12358549 10.1021/ja0261123 1:CAS:528:DC%2BD38XmvFWlt7k%3D
    • 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 12358549 10.1021/ja0261123 1:CAS:528:DC%2BD38XmvFWlt7k%3D
    • (2002) J Am Chem Soc , vol.124 , pp. 12020-12030
    • Tolman, J.R.1
  • 49
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins: Information for structure determination in solution
    • 7568117 10.1073/pnas.92.20.9279 1:CAS:528:DyaK2MXosVWltLg%3D
    • JR Tolman, et al. 1995 Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution Proc Natl Acad Sci USA 92 9279 9283 7568117 10.1073/pnas.92.20.9279 1:CAS:528:DyaK2MXosVWltLg%3D
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9279-9283
    • Tolman, J.R.1
  • 50
    • 70349910448 scopus 로고    scopus 로고
    • One-sample approach to determine the relative orientations of proteins in ternary and binary complexes from residual dipolar coupling measurements
    • 19764746 10.1021/ja904766g 1:CAS:528:DC%2BD1MXhtFCqtbrM
    • M Tonelli, et al. 2009 One-sample approach to determine the relative orientations of proteins in ternary and binary complexes from residual dipolar coupling measurements J Am Chem Soc 131 14138 14139 19764746 10.1021/ja904766g 1:CAS:528:DC%2BD1MXhtFCqtbrM
    • (2009) J Am Chem Soc , vol.131 , pp. 14138-14139
    • Tonelli, M.1
  • 51
    • 0018640809 scopus 로고
    • Fibres of highly oriented Pf1 bacteriophage produced in a strong magnetic field
    • J Torbet G Maret 1979 Fibres of highly oriented Pf1 bacteriophage produced in a strong magnetic field J Mol Biol 134 843 845 537078 10.1016/0022-2836(79)90489-3 1:CAS:528:DyaL3cXlsV2ktQ%3D%3D (Pubitemid 10133193)
    • (1979) Journal of Molecular Biology , vol.134 , Issue.4 , pp. 843-845
    • Torbet, J.1    Maret, G.2
  • 52
    • 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
    • 10.1021/ja002133q 1:CAS:528:DC%2BD3cXmt1Kisb8%3D
    • R Tycko FJ Blanco Y Ishii 2000 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 9340 9341 10.1021/ja002133q 1:CAS:528:DC%2BD3cXmt1Kisb8%3D
    • (2000) J Am Chem Soc , vol.122 , pp. 9340-9341
    • Tycko, R.1    Blanco, F.J.2    Ishii, Y.3
  • 53
    • 29544446689 scopus 로고    scopus 로고
    • Weak protein-protein interactions as probed by NMR spectroscopy
    • DOI 10.1016/j.tibtech.2005.09.006, PII S0167779905002532
    • J Vaynberg J Qin 2006 Weak protein-protein interactions as probed by NMR spectroscopy Trends Biotech 24 22 27 10.1016/j.tibtech.2005.09.006 1:CAS:528:DC%2BD28XitFCrsQ%3D%3D (Pubitemid 43017747)
    • (2006) Trends in Biotechnology , vol.24 , Issue.1 , pp. 22-27
    • Vaynberg, J.1    Qin, J.2
  • 55
    • 77955787224 scopus 로고    scopus 로고
    • Shifting the equilibrium between the encounter state and the specific form of a protein complex by interfacial point mutations
    • 20672804 10.1021/ja100867c 1:CAS:528:DC%2BC3cXpsV2lsr0%3D
    • AN Volkov Q Bashir, et al. 2010 Shifting the equilibrium between the encounter state and the specific form of a protein complex by interfacial point mutations J Am Chem Soc 132 11487 11495 20672804 10.1021/ja100867c 1:CAS:528:DC%2BC3cXpsV2lsr0%3D
    • (2010) J Am Chem Soc , vol.132 , pp. 11487-11495
    • Volkov, A.N.1    Bashir, Q.2
  • 56
    • 78651327177 scopus 로고    scopus 로고
    • Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy
    • 21049303 10.1007/s10858-010-9452-6 1:CAS:528:DC%2BC3cXhsVeku7vE
    • AN Volkov M Ubbink NAJ van Nuland 2010 Mapping the encounter state of a transient protein complex by PRE NMR spectroscopy J Biomol NMR 48 225 236 21049303 10.1007/s10858-010-9452-6 1:CAS:528:DC%2BC3cXhsVeku7vE
    • (2010) J Biomol NMR , vol.48 , pp. 225-236
    • Volkov, A.N.1    Ubbink, M.2    Van Nuland, N.A.J.3
  • 57
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • DOI 10.1021/bi011870b
    • ERP Zuiderweg 2002 Mapping protein-protein interactions in solution by NMR spectroscopy Biochemistry 41 1 7 11771996 10.1021/bi011870b 1:CAS:528:DC%2BD3MXoslygsr8%3D (Pubitemid 34049375)
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 1-7
    • Zuiderweg, E.R.P.1


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