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Volumn 55, Issue 4, 2013, Pages 311-321

BEST-TROSY experiments for time-efficient sequential resonance assignment of large disordered proteins

Author keywords

Amino acid type editing; BEST; IDP; Longitudinal relaxation enhancement; TROSY; Viral protein

Indexed keywords

AMIDE; INTRINSICALLY DISORDERED PROTEIN; NONSTRUCTURAL PROTEIN 5A; PROLINE; PROTEIN; PROTON; UNCLASSIFIED DRUG;

EID: 84877874000     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-013-9715-0     Document Type: Article
Times cited : (181)

References (33)
  • 2
    • 58049216739 scopus 로고    scopus 로고
    • Structural and dynamic characterization of intrinsically disordered human securin by NMR spectroscopy
    • 10.1021/ja805510b
    • Csizmok V, Felli IC, Tompa P, Banci L, Bertini I (2008) Structural and dynamic characterization of intrinsically disordered human securin by NMR spectroscopy. J Am Chem Soc 130:16873-16879
    • (2008) J Am Chem Soc , vol.130 , pp. 16873-16879
    • Csizmok, V.1    Felli, I.C.2    Tompa, P.3    Banci, L.4    Bertini, I.5
  • 3
    • 79952455495 scopus 로고    scopus 로고
    • How viruses hijack cell regulation
    • 10.1016/j.tibs.2010.10.002
    • Davey NE, Trave G, Gibson TJ (2011) How viruses hijack cell regulation. Trends Biochem Sci 36:159-169
    • (2011) Trends Biochem Sci , vol.36 , pp. 159-169
    • Davey, N.E.1    Trave, G.2    Gibson, T.J.3
  • 5
    • 67650525076 scopus 로고    scopus 로고
    • Longitudinal relaxation enhanced NMR experiments for the study of nucleic acids in solution
    • 10.1021/ja901633y
    • Farjon J, Boisbouvier J, Schanda P, Pardi A, Simorre JP, Brutscher B (2009) Longitudinal relaxation enhanced NMR experiments for the study of nucleic acids in solution. J Am Chem Soc 131:8571-8577
    • (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
  • 7
    • 79951549811 scopus 로고    scopus 로고
    • Recovering lost magnetization: Polarization enhancement in biomolecular NMR
    • 10.1007/s10858-010-9461-5
    • Favier A, Brutscher B (2011) Recovering lost magnetization: polarization enhancement in biomolecular NMR. J Biomol NMR 49:9-15
    • (2011) J Biomol NMR , vol.49 , pp. 9-15
    • Favier, A.1    Brutscher, B.2
  • 8
    • 67650082785 scopus 로고    scopus 로고
    • Recent advances in solution NMR: Fast methods and heteronuclear direct detection
    • 10.1002/cphc.200900133
    • Felli IC, Brutscher B (2009) Recent advances in solution NMR: fast methods and heteronuclear direct detection. Chem Phys Chem 10:1356-1368
    • (2009) Chem Phys Chem , vol.10 , pp. 1356-1368
    • Felli, I.C.1    Brutscher, B.2
  • 9
    • 84855716726 scopus 로고    scopus 로고
    • IHADAMAC: A complementary tool for sequential resonance assignment of globular and highly disordered proteins
    • 2012JMagR.214.329F 10.1016/j.jmr.2011.10.019
    • Feuerstein S, Plevin MJ, Willbold D, Brutscher B (2012a) iHADAMAC: a complementary tool for sequential resonance assignment of globular and highly disordered proteins. J Magn Reson 214:329-334
    • (2012) J Magn Reson , vol.214 , pp. 329-334
    • Feuerstein, S.1    Plevin, M.J.2    Willbold, D.3    Brutscher, B.4
  • 10
    • 84862226120 scopus 로고    scopus 로고
    • Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A
    • 10.1016/j.jmb.2012.04.023
    • Feuerstein S, Solyom Z, Aladag A, Favier A, Schwarten M, Hoffmann S, Willbold D, Brutscher B (2012b) Transient structure and SH3 interaction sites in an intrinsically disordered fragment of the hepatitis C virus protein NS5A. J Mol Biol 420:310-323
    • (2012) J Mol Biol , vol.420 , pp. 310-323
    • Feuerstein, S.1    Solyom, Z.2    Aladag, A.3    Favier, A.4    Schwarten, M.5    Hoffmann, S.6    Willbold, D.7    Brutscher, B.8
  • 11
    • 44949280676 scopus 로고
    • Band-selective radiofrequency pulses
    • Geen H, Freeman R (1991) Band-selective radiofrequency pulses. J Magn Reson 93:93-141
    • (1991) J Magn Reson , vol.93 , pp. 93-141
    • Geen, H.1    Freeman, R.2
  • 12
    • 0027569483 scopus 로고
    • Amino-acid type determination in the sequential assignment procedure of uniformly 13C/15 N-enriched porteins
    • Grzesiek S, Bax A (1993) Amino-acid type determination in the sequential assignment procedure of uniformly 13C/15 N-enriched porteins. J Biomol NMR 3:185-204
    • (1993) J Biomol NMR , vol.3 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 13
    • 77950297481 scopus 로고    scopus 로고
    • BEST-HNN and 2D-(HN)NH experiments for rapid backbone assignment in proteins
    • 2010JMagR.204.111K 10.1016/j.jmr.2010.02.013
    • Kumar D, Paul S, Hosur RV (2010) BEST-HNN and 2D-(HN)NH experiments for rapid backbone assignment in proteins. J Magn Reson 204:111-117
    • (2010) J Magn Reson , vol.204 , pp. 111-117
    • Kumar, D.1    Paul, S.2    Hosur, R.V.3
  • 14
    • 0038612578 scopus 로고
    • Wide-band excitation with polychromatic pulses
    • 10.1006/jmra.1994.1123
    • Kupce E, Freeman R (1994) Wide-band excitation with polychromatic pulses. J Magn Reson A 108:268-273
    • (1994) J Magn Reson A , vol.108 , pp. 268-273
    • Kupce, E.1    Freeman, R.2
  • 15
    • 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
    • Lescop E, Schanda P, Brutscher B (2007) A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. J Magn Reson 187:163-169 (Pubitemid 46898871)
    • (2007) Journal of Magnetic Resonance , vol.187 , Issue.1 , pp. 163-169
    • Lescop, E.1    Schanda, P.2    Brutscher, B.3
  • 16
    • 42149093129 scopus 로고    scopus 로고
    • Hadamard amino-acid-type edited NMR experiment for fast protein resonance assignment
    • DOI 10.1021/ja800914h
    • Lescop E, Rasia R, Brutscher B (2008) Hadamard amino-acid-type edited NMR experiment for fast protein resonance assignment. J Am Chem Soc 130:5014-5015 (Pubitemid 351537043)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.15 , pp. 5014-5015
    • Lescop, E.1    Rasia, R.2    Brutscher, B.3
  • 17
    • 75749113634 scopus 로고    scopus 로고
    • Guidelines for the use of band-selective radiofrequency pulses in hetero-nuclear NMR: Example of longitudinal-relaxation-enhanced BEST-type H-1-N-15 correlation experiments
    • 2010JMagR.203.190L 10.1016/j.jmr.2009.12.001
    • Lescop E, Kern T, Brutscher B (2010) Guidelines for the use of band-selective radiofrequency pulses in hetero-nuclear NMR: example of longitudinal-relaxation-enhanced BEST-type H-1-N-15 correlation experiments. J Magn Reson 203:190-198
    • (2010) J Magn Reson , vol.203 , pp. 190-198
    • Lescop, E.1    Kern, T.2    Brutscher, B.3
  • 18
    • 0034500809 scopus 로고    scopus 로고
    • HNCAN pulse sequences for sequential backbone resonance assignment across proline residues in perdeuterated proteins
    • DOI 10.1023/A:1026737732576
    • Lohr F, Pfeiffer S, Lin YJ, Hartleib J, Klimmek O, Ruterjans H (2000) HNCAN pulse sequences for sequential backbone resonance assignment across proline residues in perdeuterated proteins. J Biomol NMR 18:337-346 (Pubitemid 32065088)
    • (2000) Journal of Biomolecular NMR , vol.18 , Issue.4 , pp. 337-346
    • Lohr, F.1    Pfeiffer, S.2    Lin, Y.-J.3    Hartleib, J.4    Klimmek, O.5    Ruterjans, H.6
  • 19
    • 77954762400 scopus 로고    scopus 로고
    • HA-detected experiments for the backbone assignment of intrinsically disordered proteins
    • 10.1007/s10858-010-9421-0
    • Mantylahti S, Aitio O, Hellman M, Permi P (2010) HA-detected experiments for the backbone assignment of intrinsically disordered proteins. J Biomol NMR 47:171-181
    • (2010) J Biomol NMR , vol.47 , pp. 171-181
    • Mantylahti, S.1    Aitio, O.2    Hellman, M.3    Permi, P.4
  • 20
    • 57549105860 scopus 로고    scopus 로고
    • Detection and assignment of phosphoserine and phosphothreonine residues by (13)C-(31)P spin-echo difference NMR spectroscopy
    • 10.1007/s10858-008-9287-6
    • Mcintosh LP, Kang HS, Okon M, Nelson ML, Graves BJ, Brutscher B (2009) Detection and assignment of phosphoserine and phosphothreonine residues by (13)C-(31)P spin-echo difference NMR spectroscopy. J Biomol NMR 43:31-37
    • (2009) J Biomol NMR , vol.43 , pp. 31-37
    • McIntosh, L.P.1    Kang, H.S.2    Okon, M.3    Nelson, M.L.4    Graves, B.J.5    Brutscher, B.6
  • 21
    • 0034919873 scopus 로고    scopus 로고
    • 15N) labeled proteins: Application to unfolded proteins
    • DOI 10.1023/A:1011239023422
    • Panchal SC, Bhavesh NS, Hosur RV (2001) Improved 3D triple resonance experiments, HNN and HN(C)N, for H-N and N-15 sequential correlations in (C-13, N-15) labeled proteins: application to unfolded proteins. J Biomol NMR 20:135-147 (Pubitemid 32677757)
    • (2001) Journal of Biomolecular NMR , vol.20 , Issue.2 , pp. 135-147
    • Panchal, S.C.1    Bhavesh, N.S.2    Hosur, R.V.3
  • 22
    • 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
    • Pervushin K, Riek R, Wider G, Wüthrich K (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 (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
  • 24
    • 68049127786 scopus 로고    scopus 로고
    • Fast-pulsing longitudinal relaxation optimized techniques: Enriching the toolbox of fast biomolecular NMR spectroscopy
    • 10.1016/j.pnmrs.2009.05.002
    • Schanda P (2009) Fast-pulsing longitudinal relaxation optimized techniques: enriching the toolbox of fast biomolecular NMR spectroscopy. Prog NMR Scpectrosc 55:238-265
    • (2009) Prog NMR Scpectrosc , vol.55 , pp. 238-265
    • Schanda, P.1
  • 26
    • 0033821679 scopus 로고    scopus 로고
    • Bridging the gap: A set of selective H-1-N-15-correlations to link sequential neighbors of prolines
    • 10.1023/A:1008362904205
    • Schubert M, Ball LJ, Oschkinat H, Schmieder P (2000) Bridging the gap: a set of selective H-1-N-15-correlations to link sequential neighbors of prolines. J Biomol NMR 17:331-335
    • (2000) J Biomol NMR , vol.17 , pp. 331-335
    • Schubert, M.1    Ball, L.J.2    Oschkinat, H.3    Schmieder, P.4
  • 27
    • 0034183497 scopus 로고    scopus 로고
    • Clean TROSY: Compensation for relaxation-induced artifacts
    • 2000JMagR.144.123S 10.1006/jmre.2000.2020
    • Schulte-Herbruggen T, Sorensen OW (2000) Clean TROSY: compensation for relaxation-induced artifacts. J Magn Reson 144:123-128
    • (2000) J Magn Reson , vol.144 , pp. 123-128
    • Schulte-Herbruggen, T.1    Sorensen, O.W.2
  • 28
    • 57249085712 scopus 로고    scopus 로고
    • Improved broadband inversion performance for NMR in liquids
    • 2001JMagR.151.269S 10.1006/jmre.2001.2364
    • Smith MA, Hu H, Shaka AJ (2001) Improved broadband inversion performance for NMR in liquids. J Magn Reson 151:269-283
    • (2001) J Magn Reson , vol.151 , pp. 269-283
    • Smith, M.A.1    Hu, H.2    Shaka, A.J.3
  • 29
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • DOI 10.1016/S0968-0004(02)02169-2, PII S0968000402021692
    • Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27:527-533 (Pubitemid 35279598)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 527-533
    • Tompa, P.1
  • 30
    • 84870057622 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: A 10-year recap
    • 10.1016/j.tibs.2012.08.004
    • Tompa P (2012) Intrinsically disordered proteins: a 10-year recap. Trends Biochem Sci 37:509-516
    • (2012) Trends Biochem Sci , vol.37 , pp. 509-516
    • Tompa, P.1
  • 32
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • DOI 10.1006/jmbi.1999.3110
    • Wright PE, Dyson HJ (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J Mol Biol 293:321-331 (Pubitemid 29516173)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.2 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2


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