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Volumn 241, Issue 1, 2014, Pages 74-85

NMR contributions to structural dynamics studies of intrinsically disordered proteins

Author keywords

Biomolecular NMR; EPR spectroscopy; Intrinsically disordered proteins; NMR spin relaxation; Protein meta structure; Structural biology

Indexed keywords

ELECTRON SPIN RESONANCE SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; STRUCTURAL DYNAMICS; X RAY CRYSTALLOGRAPHY;

EID: 84896919406     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2013.11.011     Document Type: Article
Times cited : (145)

References (58)
  • 1
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • H.J. Dyson, and P.E. Wright Unfolded proteins and protein folding studied by NMR Chem. Rev. 104 2004 3607 3622
    • (2004) Chem. Rev. , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 5
    • 84868115572 scopus 로고    scopus 로고
    • Exclusively heteronuclear (13) C-detected amino-acid-selective NMR experiments for the study of intrinsically disordered proteins (IDPs)
    • W. Bermel, I. Bertini, J. Chill, I.C. Felli, N. Haba, M.V.V. Kumar, and R. Pierattelli Exclusively heteronuclear (13) C-detected amino-acid-selective NMR experiments for the study of intrinsically disordered proteins (IDPs) ChemBioChem 13 2012 2425 2432
    • (2012) ChemBioChem , vol.13 , pp. 2425-2432
    • Bermel, W.1    Bertini, I.2    Chill, J.3    Felli, I.C.4    Haba, N.5    Kumar, M.V.V.6    Pierattelli, R.7
  • 6
    • 80053584880 scopus 로고    scopus 로고
    • High-resolution characterization of intrinsic disorder in proteins: Expanding the suite of (13)C-detected NMR spectroscopy experiments to determine key observables
    • I. Bertini, I.C. Felli, L. Gonnelli, M.V. Vasantha Kumar, and R. Pierattelli High-resolution characterization of intrinsic disorder in proteins: expanding the suite of (13)C-detected NMR spectroscopy experiments to determine key observables ChemBioChem 12 2011 2347 2352
    • (2011) ChemBioChem , vol.12 , pp. 2347-2352
    • Bertini, I.1    Felli, I.C.2    Gonnelli, L.3    Vasantha Kumar, M.V.4    Pierattelli, R.5
  • 7
    • 77955304413 scopus 로고    scopus 로고
    • Non-uniform frequency domain for optimal exploitation of non-uniform sampling
    • K. Kazimierczuk, A. Zawadzka-Kazimierczuk, and W. Kozminski Non-uniform frequency domain for optimal exploitation of non-uniform sampling J. Magn. Reson. 205 2010 286 292
    • (2010) J. Magn. Reson. , vol.205 , pp. 286-292
    • Kazimierczuk, K.1    Zawadzka-Kazimierczuk, A.2    Kozminski, W.3
  • 9
    • 84863104592 scopus 로고    scopus 로고
    • High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
    • A. Zawadzka-Kazimierczuk, W. Kozminski, H. Sanderova, and L. Krasny High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins J. Biomol. NMR 52 2012 329 337
    • (2012) J. Biomol. NMR , vol.52 , pp. 329-337
    • Zawadzka-Kazimierczuk, A.1    Kozminski, W.2    Sanderova, H.3    Krasny, L.4
  • 10
    • 84877874000 scopus 로고    scopus 로고
    • BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins
    • Z. Solyom, M. Schwarten, L. Geist, R. Konrat, D. Willbold, and B. Brutscher BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins J. Biomol. NMR 55 2013 311 321
    • (2013) J. Biomol. NMR , vol.55 , pp. 311-321
    • Solyom, Z.1    Schwarten, M.2    Geist, L.3    Konrat, R.4    Willbold, D.5    Brutscher, B.6
  • 11
    • 84884241538 scopus 로고    scopus 로고
    • Conformational propensities of intrinsically disordered proteins from NMR chemical shifts
    • J. Kragelj, V. Ozenne, M. Blackledge, and M.R. Jensen Conformational propensities of intrinsically disordered proteins from NMR chemical shifts ChemPhysChem 14 2013 3034 3045
    • (2013) ChemPhysChem , vol.14 , pp. 3034-3045
    • Kragelj, J.1    Ozenne, V.2    Blackledge, M.3    Jensen, M.R.4
  • 12
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between α- and γ-synuclein: Implications for fibrillation
    • DOI 10.1110/ps.062465306
    • J.A. Marsh, V.K. Singh, Z. Jia, and J.D. Forman-Kay Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation Protein Sci. 15 2006 2795 2804 (Pubitemid 44833760)
    • (2006) Protein Science , vol.15 , Issue.12 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 13
    • 84858634014 scopus 로고    scopus 로고
    • Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts
    • C. Camilloni, A. De Simone, W.F. Vranken, and M. Vendruscolo Determination of secondary structure populations in disordered states of proteins using nuclear magnetic resonance chemical shifts Biochemistry 51 2012 2224 2231
    • (2012) Biochemistry , vol.51 , pp. 2224-2231
    • Camilloni, C.1    De Simone, A.2    Vranken, W.F.3    Vendruscolo, M.4
  • 14
    • 84866704850 scopus 로고    scopus 로고
    • Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins
    • K. Tamiola, and F.A. Mulder Using NMR chemical shifts to calculate the propensity for structural order and disorder in proteins Biochem. Soc. Trans. 40 2012 1014 1020
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 1014-1020
    • Tamiola, K.1    Mulder, F.A.2
  • 15
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • DOI 10.1006/jmbi.2001.4750
    • W.Y. Choy, and J.D. Forman-Kay Calculation of ensembles of structures representing the unfolded state of an SH3 domain J. Mol. Biol. 308 2001 1011 1032 (Pubitemid 32577079)
    • (2001) Journal of Molecular Biology , vol.308 , Issue.5 , pp. 1011-1032
    • Choy, W.-Y.1    Forman-Kay, J.D.2
  • 16
    • 77958510026 scopus 로고    scopus 로고
    • Modeling intrinsically disordered proteins with bayesian statistics
    • C.K. Fisher, A. Huang, and C.M. Stultz Modeling intrinsically disordered proteins with bayesian statistics J. Am. Chem. Soc. 132 2010 14919 14927
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 14919-14927
    • Fisher, C.K.1    Huang, A.2    Stultz, C.M.3
  • 17
    • 79958037883 scopus 로고    scopus 로고
    • Constructing ensembles for intrinsically disordered proteins
    • C.K. Fisher, and C.M. Stultz Constructing ensembles for intrinsically disordered proteins Curr. Opin. Struct. Biol. 21 2011 426 431
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 426-431
    • Fisher, C.K.1    Stultz, C.M.2
  • 18
    • 84861736272 scopus 로고    scopus 로고
    • Flexible-meccano: A tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables
    • V. Ozenne, F. Bauer, L. Salmon, J.R. Huang, M.R. Jensen, S. Segard, P. Bernado, C. Charavay, and M. Blackledge Flexible-meccano: a tool for the generation of explicit ensemble descriptions of intrinsically disordered proteins and their associated experimental observables Bioinformatics 28 2012 1463 1470
    • (2012) Bioinformatics , vol.28 , pp. 1463-1470
    • Ozenne, V.1    Bauer, F.2    Salmon, L.3    Huang, J.R.4    Jensen, M.R.5    Segard, S.6    Bernado, P.7    Charavay, C.8    Blackledge, M.9
  • 19
    • 33846913510 scopus 로고    scopus 로고
    • Atomic-level characterization of disordered protein ensembles
    • DOI 10.1016/j.sbi.2007.01.009, PII S0959440X07000103, Foldinf and Binding / Protein-Nucleic Interactions
    • T. Mittag, and J.D. Forman-Kay Atomic-level characterization of disordered protein ensembles Curr. Opin. Struct. Biol. 17 2007 3 14 (Pubitemid 46240819)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 3-14
    • Mittag, T.1    Forman-Kay, J.D.2
  • 20
    • 34547679071 scopus 로고    scopus 로고
    • NMR: Prediction of protein flexibility
    • M. Berjanskii, and D.S. Wishart NMR: prediction of protein flexibility Nat. Protoc. 1 2006 683 688
    • (2006) Nat. Protoc. , vol.1 , pp. 683-688
    • Berjanskii, M.1    Wishart, D.S.2
  • 21
    • 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, and A. Bax Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium Science 278 1997 1111 1114 (Pubitemid 27517889)
    • (1997) Science , vol.278 , Issue.5340 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 22
    • 3242789489 scopus 로고    scopus 로고
    • Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings
    • DOI 10.1016/j.jmb.2004.05.022, PII S0022283604005881
    • R. Mohana-Borges, N.K. Goto, G.J. Kroon, H.J. Dyson, and P.E. Wright Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings J. Mol. Biol. 340 2004 1131 1142 (Pubitemid 38968706)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.5 , pp. 1131-1142
    • Mohana-Borges, R.1    Goto, N.K.2    Kroon, G.J.A.3    Dyson, H.J.4    Wright, P.E.5
  • 26
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • DOI 10.1016/0076-6879(89)77007-5
    • P.A. Kosen Spin labeling of proteins Methods Enzymol. 177 1989 86 121 (Pubitemid 20041572)
    • (1989) Methods in Enzymology , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 27
    • 77952915958 scopus 로고    scopus 로고
    • Protein NMR using paramagnetic ions
    • G. Otting Protein NMR using paramagnetic ions Annu. Rev. Biophys. 39 2010 387 405
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 387-405
    • Otting, G.1
  • 28
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data
    • DOI 10.1021/bi000060h
    • J.L. Battiste, and G. Wagner Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data Biochemistry 39 2000 5355 5365 (Pubitemid 30257075)
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 30
    • 73249124356 scopus 로고    scopus 로고
    • Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements
    • J.R. Allison, P. Varnai, C.M. Dobson, and M. Vendruscolo Determination of the free energy landscape of alpha-synuclein using spin label nuclear magnetic resonance measurements J. Am. Chem. Soc. 131 2009 18314 18326
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 18314-18326
    • Allison, J.R.1    Varnai, P.2    Dobson, C.M.3    Vendruscolo, M.4
  • 31
    • 80053517890 scopus 로고    scopus 로고
    • Structural impact of proline-directed pseudophosphorylation at AT8, AT100, and PHF1 epitopes on 441-residue tau
    • S. Bibow, V. Ozenne, J. Biernat, M. Blackledge, E. Mandelkow, and M. Zweckstetter Structural impact of proline-directed pseudophosphorylation at AT8, AT100, and PHF1 epitopes on 441-residue tau J. Am. Chem. Soc. 133 2011 15842 15845
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15842-15845
    • Bibow, S.1    Ozenne, V.2    Biernat, J.3    Blackledge, M.4    Mandelkow, E.5    Zweckstetter, M.6
  • 33
    • 77956332835 scopus 로고    scopus 로고
    • Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators
    • J.A. Marsh, B. Dancheck, M.J. Ragusa, M. Allaire, J.D. Forman-Kay, and W. Peti Structural diversity in free and bound states of intrinsically disordered protein phosphatase 1 regulators Structure 18 2010 1094 1103
    • (2010) Structure , vol.18 , pp. 1094-1103
    • Marsh, J.A.1    Dancheck, B.2    Ragusa, M.J.3    Allaire, M.4    Forman-Kay, J.D.5    Peti, W.6
  • 34
    • 70449534683 scopus 로고    scopus 로고
    • The protein meta-structure: A novel concept for chemical and molecular biology
    • R. Konrat The protein meta-structure: a novel concept for chemical and molecular biology Cell. Mol. Life Sci. 66 2009 3625 3639
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 3625-3639
    • Konrat, R.1
  • 35
    • 84857711352 scopus 로고    scopus 로고
    • Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope
    • C. Mayer, L. Slater, M.C. Erat, R. Konrat, and I. Vakonakis Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope J. Biol. Chem. 287 2012 7182 7189
    • (2012) J. Biol. Chem. , vol.287 , pp. 7182-7189
    • Mayer, C.1    Slater, L.2    Erat, M.C.3    Konrat, R.4    Vakonakis, I.5
  • 38
    • 33646358424 scopus 로고    scopus 로고
    • HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains
    • P. Schanda, V. Forge, and B. Brutscher HET-SOFAST NMR for fast detection of structural compactness and heterogeneity along polypeptide chains Magn. Reson. Chem. 44 Spec No 2006 S177 S184
    • (2006) Magn. Reson. Chem. , vol.44
    • Schanda, P.1    Forge, V.2    Brutscher, B.3
  • 39
    • 0033037209 scopus 로고    scopus 로고
    • 15N-T(1π) dispersion during adiabatic fast passage
    • DOI 10.1023/A:1008324721356
    • R. Konrat, and M. Tollinger Heteronuclear relaxation in time-dependent spin systems: N-15-T-1 rho dispersion during adiabatic fast passage J. Biomol. NMR 13 1999 213 221 (Pubitemid 29143529)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 213-221
    • Konrat, R.1    Tollinger, M.2
  • 41
    • 77955327536 scopus 로고    scopus 로고
    • Intrinsically disordered proteins are potential drug targets
    • S.J. Metallo Intrinsically disordered proteins are potential drug targets Curr. Opin. Chem. Biol. 14 2010 481 488
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 481-488
    • Metallo, S.J.1
  • 42
    • 84866309681 scopus 로고    scopus 로고
    • Toward rational fragment-based lead design without 3D structures
    • M.A. Henen, N. Coudevylle, L. Geist, and R. Konrat Toward rational fragment-based lead design without 3D structures J. Med. Chem. 55 2012 7909 7919
    • (2012) J. Med. Chem. , vol.55 , pp. 7909-7919
    • Henen, M.A.1    Coudevylle, N.2    Geist, L.3    Konrat, R.4
  • 44
    • 84876469036 scopus 로고    scopus 로고
    • Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation
    • J. Stanek, S. Saxena, L. Geist, R. Konrat, and W. Kozminski Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation Angew. Chem., Int. Ed. Engl. 52 2013 4604 4606
    • (2013) Angew. Chem., Int. Ed. Engl. , vol.52 , pp. 4604-4606
    • Stanek, J.1    Saxena, S.2    Geist, L.3    Konrat, R.4    Kozminski, W.5
  • 45
    • 0036234486 scopus 로고    scopus 로고
    • Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation
    • DOI 10.1023/A:1014936319712
    • K. Kloiber, W. Schuler, and R. Konrat Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation J. Biomol. NMR 22 2002 349 363 (Pubitemid 34449946)
    • (2002) Journal of Biomolecular NMR , vol.22 , Issue.4 , pp. 349-363
    • Kloiber, K.1    Schuler, W.2    Konrat, R.3
  • 46
    • 84881258864 scopus 로고    scopus 로고
    • Cooperative unfolding of compact conformations of the intrinsically disordered protein Osteopontin
    • D. Kurzbach, G. Platzer, T.C. Schwarz, M.A. Henen, R. Konrat, and D. Hinderberger Cooperative unfolding of compact conformations of the intrinsically disordered protein Osteopontin Biochemistry 52 2013 5167 5175
    • (2013) Biochemistry , vol.52 , pp. 5167-5175
    • Kurzbach, D.1    Platzer, G.2    Schwarz, T.C.3    Henen, M.A.4    Konrat, R.5    Hinderberger, D.6
  • 47
    • 33645914006 scopus 로고
    • A model-free approach to the interpretation of Nmr relaxation in macromolecules
    • G. Lipari, and A. Szabo A model-free approach to the interpretation of Nmr relaxation in macromolecules Biophys. J. 33 1981 A307-A307
    • (1981) Biophys. J. , vol.33
    • Lipari, G.1    Szabo, A.2
  • 48
    • 70350348011 scopus 로고    scopus 로고
    • NMR spectroscopy brings invisible protein states into focus
    • A.J. Baldwin, and L.E. Kay NMR spectroscopy brings invisible protein states into focus Nat. Chem. Biol. 5 2009 808 814
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 808-814
    • Baldwin, A.J.1    Kay, L.E.2
  • 49
    • 70350091410 scopus 로고    scopus 로고
    • Domain-elongation NMR spectroscopy yields new insights into RNA dynamics and adaptive recognition
    • Q. Zhang, and H.M. Al-Hashimi Domain-elongation NMR spectroscopy yields new insights into RNA dynamics and adaptive recognition RNA 15 2009 1941 1948
    • (2009) RNA , vol.15 , pp. 1941-1948
    • Zhang, Q.1    Al-Hashimi, H.M.2
  • 51
    • 0017309766 scopus 로고
    • Structural patterns in globular proteins
    • M. Levitt, and C. Chothia Structural patterns in globular proteins Nature 261 1976 552 558
    • (1976) Nature , vol.261 , pp. 552-558
    • Levitt, M.1    Chothia, C.2
  • 54
    • 84886688567 scopus 로고    scopus 로고
    • Detecting repetitions and periodicities in proteins by tiling the structural space
    • R.G. Parra, R. Espada, I.E. Sanchez, M.J. Sippl, and D.U. Ferreiro Detecting repetitions and periodicities in proteins by tiling the structural space J. Phys. Chem. B 117 2013 12887 12897
    • (2013) J. Phys. Chem. B , vol.117 , pp. 12887-12897
    • Parra, R.G.1    Espada, R.2    Sanchez, I.E.3    Sippl, M.J.4    Ferreiro, D.U.5
  • 57
    • 0032993447 scopus 로고    scopus 로고
    • Polymer principles and protein folding
    • K.A. Dill Polymer principles and protein folding Protein Sci. 8 1999 1166 1180 (Pubitemid 29264947)
    • (1999) Protein Science , vol.8 , Issue.6 , pp. 1166-1180
    • Dill, K.A.1
  • 58
    • 38849092210 scopus 로고    scopus 로고
    • A note on difficult structure alignment problems
    • DOI 10.1093/bioinformatics/btm622
    • M.J. Sippl, and M. Wiederstein A note on difficult structure alignment problems Bioinformatics 24 2008 426 427 (Pubitemid 351189021)
    • (2008) Bioinformatics , vol.24 , Issue.3 , pp. 426-427
    • Sippl, M.J.1    Wiederstein, M.2


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