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Volumn 239, Issue , 2014, Pages 23-28

Sequential protein NMR assignments in the liquid state via sequential data acquisition

Author keywords

Minichromosome maintenance (MCM); NMR; Protein resonance assignment; Sequential data acquisition; Winged helix domain (WH)

Indexed keywords

CHEMICAL SHIFT CORRELATION SPECTRA; LABELLED PROTEIN; MINICHROMOSOME MAINTENANCE (MCM); PROTEIN NMR ASSIGNMENT; RESONANCE ASSIGNMENTS; SEQUENTIAL RESONANCE ASSIGNMENTS; SULFOLOBUS SOLFATARICUS; WINGED HELIX DOMAIN (WH);

EID: 84891523377     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2013.12.002     Document Type: Article
Times cited : (16)

References (29)
  • 1
    • 43949167657 scopus 로고
    • HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins
    • M. Wittekind, and L. Mueller HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins J. Magnet. Reson. Ser. B 101 2 1993 201 205
    • (1993) J. Magnet. Reson. Ser. B , vol.101 , Issue.2 , pp. 201-205
    • Wittekind, M.1    Mueller, L.2
  • 2
    • 0027569483 scopus 로고
    • Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins
    • S. Grzesiek, and A. Bax Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins J. Biomol. NMR 3 2 1993 185 204
    • (1993) J. Biomol. NMR , vol.3 , Issue.2 , pp. 185-204
    • Grzesiek, S.1    Bax, A.2
  • 3
    • 0030137565 scopus 로고    scopus 로고
    • α pulses for improvement of HN(CA)CO-D and HN(COCA)NH-D experiments
    • H. Matsuo, E. Kupče, H. Li, and G. Wagner Use of selective C α pulses for improvement of HN (CA) CO-D and HN (COCA) NH-D experiments J. Magnet. Reson. Ser. B 111 2 1996 194 198 (Pubitemid 126758679)
    • (1996) Journal of Magnetic Resonance - Series B , vol.111 , Issue.2 , pp. 194-198
    • Matsuo, H.1    Kupce, E.2    Li, H.3    Wagner, G.4
  • 5
    • 0042964750 scopus 로고
    • COCONOSY. Combination of 2D correlated and 2D nuclear overhauser enhancement spectroscopy in a single experiment
    • C. Haasnoot, F. Van de Ven, and C. Hilbers COCONOSY. Combination of 2D correlated and 2D nuclear overhauser enhancement spectroscopy in a single experiment J. Magnet. Reson. (1969) 56 2 1984 343 349
    • (1984) J. Magnet. Reson. (1969) , vol.56 , Issue.2 , pp. 343-349
    • Haasnoot, C.1    Van De Ven, F.2    Hilbers, C.3
  • 8
    • 84865660352 scopus 로고    scopus 로고
    • Parallel acquisition of multi-dimensional spectra in protein NMR
    • Ě.E. Kupče, and L.E.L. Kay Parallel acquisition of multi-dimensional spectra in protein NMR J. Biomol. NMR 54 1 2012 1 7
    • (2012) J. Biomol. NMR , vol.54 , Issue.1 , pp. 1-7
    • Kupče, Ě.E.1    Kay, L.E.L.2
  • 9
    • 84879841598 scopus 로고    scopus 로고
    • Parallel acquisition of 3D-HA(CA)NH and 3D-HACACO spectra
    • J.G. Reddy, and R.V. Hosur Parallel acquisition of 3D-HA(CA)NH and 3D-HACACO spectra J. Biomol. NMR 56 2 2013 77 84
    • (2013) J. Biomol. NMR , vol.56 , Issue.2 , pp. 77-84
    • Reddy, J.G.1    Hosur, R.V.2
  • 10
    • 0009195494 scopus 로고
    • The use of heteronuclear cross polarization to enhance the sensitivity of triple-resonance NMR experiments. Improved 4D HCNNH pulse sequences
    • J.M. Richardson, R.T. Clowes, W. Boucher, P.J. Domaille, C.H. Hardman, J. Keeler, and E.D. Laue The use of heteronuclear cross polarization to enhance the sensitivity of triple-resonance NMR experiments. Improved 4D HCNNH pulse sequences J. Magnet. Reson., Series B 101 2 1993 223 227
    • (1993) J. Magnet. Reson., Series B , vol.101 , Issue.2 , pp. 223-227
    • Richardson, J.M.1    Clowes, R.T.2    Boucher, W.3    Domaille, P.J.4    Hardman, C.H.5    Keeler, J.6    Laue, E.D.7
  • 11
    • 0026619586 scopus 로고
    • Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments
    • DOI 10.1016/0014-5793(92)81517-P
    • T.M. Logan, E.T. Olejniczak, R.X. Xu, and S.W. Fesik Side chain and backbone assignments in isotopically labeled proteins from two heteronuclear triple resonance experiments FEBS Lett. 314 3 1992 413 418 (Pubitemid 23005701)
    • (1992) FEBS Letters , vol.314 , Issue.3 , pp. 413-418
    • Logan, T.M.1    Olejniczak, E.T.2    Xu, R.X.3    Fesik, S.W.4
  • 12
    • 0001590904 scopus 로고
    • An HCCNH triple-resonance experiment using carbon-13 isotropic mixing for correlating backbone amide and side-chain aliphatic resonances in isotopically enriched proteins
    • B.A. Lyons, and G.T. Montelione An HCCNH triple-resonance experiment using carbon-13 isotropic mixing for correlating backbone amide and side-chain aliphatic resonances in isotopically enriched proteins J. Magnet. Reson., Series B 101 2 1993 206 209
    • (1993) J. Magnet. Reson., Series B , vol.101 , Issue.2 , pp. 206-209
    • Lyons, B.A.1    Montelione, G.T.2
  • 14
    • 84858058799 scopus 로고    scopus 로고
    • Dual acquisition magic-angle spinning solid-state NMR-spectroscopy: Simultaneous acquisition of multidimensional spectra of biomacromolecules
    • T.T. Gopinath, and G.G. Veglia Dual acquisition magic-angle spinning solid-state NMR-spectroscopy: simultaneous acquisition of multidimensional spectra of biomacromolecules Angewandte Chemie (International ed in English) 51 11 2012 2731 2735
    • (2012) Angewandte Chemie (International Ed in English) , vol.51 , Issue.11 , pp. 2731-2735
    • Gopinath, T.T.1    Veglia, G.G.2
  • 15
    • 84874499532 scopus 로고    scopus 로고
    • Solid state NMR of proteins at high MAS frequencies: Symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra
    • P. Bellstedt, C. Herbst, S. Häfner, J. Leppert, M. Görlach, and R. Ramachandran Solid state NMR of proteins at high MAS frequencies: symmetry-based mixing and simultaneous acquisition of chemical shift correlation spectra J. Biomol. NMR 54 4 2012 325 335
    • (2012) J. Biomol. NMR , vol.54 , Issue.4 , pp. 325-335
    • Bellstedt, P.1    Herbst, C.2    Häfner, S.3    Leppert, J.4    Görlach, M.5    Ramachandran, R.6
  • 16
    • 84862697344 scopus 로고    scopus 로고
    • Utilizing afterglow magnetization from cross-polarization magic-angle-spinning solid-state NMR spectroscopy to obtain simultaneous heteronuclear multidimensional spectra
    • J.R.J. Banigan, and N.J.N. Traaseth Utilizing afterglow magnetization from cross-polarization magic-angle-spinning solid-state NMR spectroscopy to obtain simultaneous heteronuclear multidimensional spectra J. Phys. Chem. B 116 24 2012 7138 7144
    • (2012) J. Phys. Chem. B , vol.116 , Issue.24 , pp. 7138-7144
    • Banigan, J.R.J.1    Traaseth, N.J.N.2
  • 19
    • 2642628181 scopus 로고
    • A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants
    • D. States, R. Haberkorn, and D. Ruben A two-dimensional nuclear overhauser experiment with pure absorption phase in four quadrants J. Magnet. Reson. (1969) 48 2 1982 286 292
    • (1982) J. Magnet. Reson. (1969) , vol.48 , Issue.2 , pp. 286-292
    • States, D.1    Haberkorn, R.2    Ruben, D.3
  • 20
    • 84924408303 scopus 로고    scopus 로고
    • (1)H,(15)N and (13)C chemical shift assignments for the winged helix domains of two archeal MCM C-termini
    • doi:10.1007/s12104-013-9516-0 doi
    • C. Wiedemann, O. OhlenschlSger, B. Medagli, S. Onesti, M. Görlach, (1)H,(15)N and (13)C chemical shift assignments for the winged helix domains of two archeal MCM C-termini, Biomol. NMR Assign., doi: http://dx.doi.org/10.1007/ s12104-013-9516-0.
    • Biomol. NMR Assign
    • Wiedemann, C.1
  • 21
    • 0026610868 scopus 로고
    • 15N NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteins
    • 15N NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteins Biochemistry 31 27 1992 6254 6265
    • (1992) Biochemistry , vol.31 , Issue.27 , pp. 6254-6265
    • Wittekind, M.1    Görlach, M.2    Friedrichs, M.3    Dreyfuss, G.4    Mueller, L.5
  • 23
    • 0000827947 scopus 로고
    • The use of heteronuclear cross-polarization for backbone assignment of (2)H-, (15)N- and (13)C-labeled proteins: A pulse scheme for triple-resonance 4D correlation of sequential amide protons and (15)N
    • M. Shirakawa, M. WSlchli, M. Shimizu, and Y. Kyogoku The use of heteronuclear cross-polarization for backbone assignment of (2)H-, (15)N- and (13)C-labeled proteins: a pulse scheme for triple-resonance 4D correlation of sequential amide protons and (15)N J. Biomol. NMR 5 3 1995 323 326
    • (1995) J. Biomol. NMR , vol.5 , Issue.3 , pp. 323-326
    • Shirakawa, M.1    Wslchli, M.2    Shimizu, M.3    Kyogoku, Y.4
  • 24
    • 0000061511 scopus 로고
    • 15N-enriched proteins. Application to triple resonance 4D J connectivity of sequential amides
    • 15N-enriched proteins. Application to triple resonance 4D J connectivity of sequential amides J. Am. Chem. Soc. 115 10 1993 4369 4370
    • (1993) J. Am. Chem. Soc. , vol.115 , Issue.10 , pp. 4369-4370
    • Grzesiek, S.1    Anglister, J.2    Ren, H.3    Bax, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.