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Volumn 54, Issue 4, 2012, Pages 343-353

Spectral editing of two-dimensional magic-angle-spinning solid-state NMR spectra for protein resonance assignment and structure determination

Author keywords

CH selection; Protein secondary structure; REDOR; Spectral editing

Indexed keywords

ASPARTIC ACID; CARBENE; CARBOXYL GROUP; GLUTAMIC ACID; ISOLEUCINE; UBIQUITIN; VALINE;

EID: 84874451281     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-012-9676-8     Document Type: Article
Times cited : (30)

References (48)
  • 1
    • 0001552551 scopus 로고    scopus 로고
    • Repulsion, a novel approach to efficient powder averaging in solid-state NMR
    • Bak M, Nielsen NC (1997) REPULSION, a novel approach to efficient powder averaging in solid-state NMR. J Magn Reson 125:132-139 (Pubitemid 127451359)
    • (1997) Journal of Magnetic Resonance , vol.125 , Issue.1 , pp. 132-139
    • Bak, M.1    Nielsen, N.Chr.2
  • 2
    • 48749145034 scopus 로고
    • Chemical shift anisotropy in powdered solids studied by 2D Fourier transform NMR with flipping of the spinning axis
    • Bax A, Szeverenyi NM, Maciel GE (1983) Chemical shift anisotropy in powdered solids studied by 2D Fourier transform NMR with flipping of the spinning axis. J Magn Reson 55:494-497
    • (1983) J Magn Reson , vol.55 , pp. 494-497
    • Bax, A.1    Szeverenyi, N.M.2    MacIel, G.E.3
  • 3
    • 0002377859 scopus 로고
    • Frequency-switched pulse sequences: Homonuclear decoupling and dilute spin NMR in solids
    • 1989CPL.155.341B 10.1016/0009-2614(89)87166-0
    • Bielecki A, Kolbert AC, Levitt MH (1989) Frequency-switched pulse sequences: homonuclear decoupling and dilute spin NMR in solids. Chem Phys Lett 155:341-346
    • (1989) Chem Phys Lett , vol.155 , pp. 341-346
    • Bielecki, A.1    Kolbert, A.C.2    Levitt, M.H.3
  • 4
    • 0037038365 scopus 로고    scopus 로고
    • Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy
    • DOI 10.1038/nature01070
    • Castellani F, vanRossum B, Diehl A, Schubert M, Rehbein K, Oschkinat H (2002) Structure of a protein determined by solid-state magic-angle spinning NMR spectroscopy. Nature 420:98-102 (Pubitemid 35291447)
    • (2002) Nature , vol.420 , Issue.6911 , pp. 98-102
    • Castellani, F.1    Van Rossum, B.2    Diehl, A.3    Schubert, M.4    Rehbein, K.5    Oschklnat, H.6
  • 5
    • 0035743932 scopus 로고    scopus 로고
    • Spectral editing in (13)C MAS NMR under moderately fast spinning conditions
    • 2001JMagR.148.327D 10.1006/jmre.2000.2255
    • De Vita E, Frydman L (2001) Spectral editing in (13)C MAS NMR under moderately fast spinning conditions. J Magn Reson 148:327-337
    • (2001) J Magn Reson , vol.148 , pp. 327-337
    • De Vita, E.1    Frydman, L.2
  • 6
    • 33846430490 scopus 로고    scopus 로고
    • Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy
    • DOI 10.1002/anie.200602139
    • Etzkorn M, Martell S, Andronesi OC, Seidel K, Engelhard M, Baldus M (2007) Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy. Angew Chem Int Ed Engl 46:459-462 (Pubitemid 46142261)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.3 , pp. 459-462
    • Etzkorn, M.1    Martell, S.2    Andronesi, O.C.3    Seidel, K.4    Engelhard, M.5    Baldus, M.6
  • 7
    • 72449152678 scopus 로고    scopus 로고
    • Fate of the amino acid in glucose-glycine melanoidins investigated by solid-state nuclear magnetic resonance
    • 10.1021/jf9020587
    • Fang XW, Schmidt-Rohr K (2009) Fate of the amino acid in glucose-glycine melanoidins investigated by solid-state nuclear magnetic resonance. J Agric Food Chem 57:10701-10711
    • (2009) J Agric Food Chem , vol.57 , pp. 10701-10711
    • Fang, X.W.1    Schmidt-Rohr, K.2
  • 11
    • 0021286554 scopus 로고
    • 13C spin exchange in amino acids and peptides
    • 10.1021/ja00329a052
    • Frey MH, Opella SJ (1984) 13C spin exchange in amino acids and peptides. J Am Chem Soc 106:4942-4945
    • (1984) J Am Chem Soc , vol.106 , pp. 4942-4945
    • Frey, M.H.1    Opella, S.J.2
  • 12
    • 0028354429 scopus 로고
    • Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR
    • Gallagher T, Alexander P, Bryan P, Gilliland GL (1994) Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR. Biochemistry 33:4721-4729 (Pubitemid 24145123)
    • (1994) Biochemistry , vol.33 , Issue.15 , pp. 4721-4729
    • Gallagher, T.1    Alexander, P.2    Bryan, P.3    Gilliland, G.L.4
  • 14
    • 45149145322 scopus 로고
    • Rotational echo double resonance NMR
    • Gullion T, Schaefer J (1989) Rotational echo double resonance NMR. J Magn Reson 81:196-200
    • (1989) J Magn Reson , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 15
    • 3242887525 scopus 로고    scopus 로고
    • STRIDE: A web server for secondary structure assignment from known atomic coordinates of proteins
    • Web Server Issue
    • Heinig M, Frishman D (2004) STRIDE: a web server for secondary structure assignment from known atomic coordinates of proteins. Nucleic Acids Res 32, Web Server Issue
    • (2004) Nucleic Acids Res 32
    • Heinig, M.1    Frishman, D.2
  • 16
    • 0242499504 scopus 로고    scopus 로고
    • Bone recognition mechanism of porcine osteocalcin from crystal structure
    • DOI 10.1038/nature02079
    • Hoang QQ, Sicheri F, Howard AJ, Yang DSC (2003) Bone recognition mechanism of porcine osteocalcin from crystal structure. Nature 425:977-980 (Pubitemid 37376930)
    • (2003) Nature , vol.425 , Issue.6961 , pp. 977-980
    • Hoang, Q.Q.1    Sicheri, F.2    Howard, A.J.3    Yang, D.S.C.4
  • 17
    • 33845217043 scopus 로고    scopus 로고
    • Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR
    • DOI 10.1016/j.str.2006.10.002, PII S0969212606004011
    • Hong M (2006) Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR. Structure 14:1731-1740 (Pubitemid 44855624)
    • (2006) Structure , vol.14 , Issue.12 , pp. 1731-1740
    • Hong, M.1
  • 18
    • 84859912916 scopus 로고    scopus 로고
    • Membrane protein structure and dynamics from NMR spectroscopy
    • 2012ARPC.63.1H 10.1146/annurev-physchem-032511-143731
    • Hong M, Zhang Y, Hu F (2012) Membrane protein structure and dynamics from NMR spectroscopy. Annu Rev Phys Chem 63:1-24
    • (2012) Annu Rev Phys Chem , vol.63 , pp. 1-24
    • Hong, M.1    Zhang, Y.2    Hu, F.3
  • 19
    • 0035954376 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain
    • Huster D, Xiao LS, Hong M (2001) Solid-state NMR investigation of the dynamics of colicin Ia channel-forming domain. Biochemistry 40:7662-7674 (Pubitemid 32578030)
    • (2001) Biochemistry , vol.40 , Issue.25 , pp. 7662-7674
    • Huster, D.1    Xiao, L.2    Hong, M.3
  • 21
    • 33750979282 scopus 로고    scopus 로고
    • Spectral editing: Selection of methyl groups in multidimensional solid-state magic-angle spinning NMR
    • DOI 10.1007/s10858-006-9078-x
    • Jehle S, Hiller M, Rehbein K, Diehl A, Oschkinat H, van Rossum BJ (2006a) Spectral editing: selection of methyl groups in multidimensional solid-state magic-angle spinning NMR. J Biomol NMR 36:169-177 (Pubitemid 44740880)
    • (2006) Journal of Biomolecular NMR , vol.36 , Issue.3 , pp. 169-177
    • Jehle, S.1    Hiller, M.2    Rehbein, K.3    Diehl, A.4    Oschkinat, H.5    Rossum, B.-J.6
  • 22
    • 33750934162 scopus 로고    scopus 로고
    • 15N labeled proteins by MAS NMR: Filtering of lysines and arginines
    • DOI 10.1016/j.jmr.2006.08.015, PII S1090780706002722
    • Jehle S, Rehbein K, Diehl A, van Rossum BJ (2006b) Amino-acid selective experiments on uniformly 13C and 15N labeled proteins by MAS NMR: filtering of lysines and arginines. J Magn Reson 183:324-328 (Pubitemid 44739344)
    • (2006) Journal of Magnetic Resonance , vol.183 , Issue.2 , pp. 324-328
    • Jehle, S.1    Rehbein, K.2    Diehl, A.3    Van Rossum, B.-J.4
  • 23
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • 10.1002/bip.360221211
    • Kabsch W, Sander C (1983) Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 24
    • 0034609433 scopus 로고    scopus 로고
    • 13C NMR spectral editing of humic material
    • 10.1016/S0022-2860(00)00501-9
    • 13C NMR spectral editing of humic material. J Mol Struct 550-551:297-305
    • (2000) J Mol Struct , vol.550-551 , pp. 297-305
    • Keeler, C.1    MacIel, G.E.2
  • 25
    • 0032558077 scopus 로고    scopus 로고
    • Carbon-13 spectral editing in solid-state NMR using heteronuclear scalar couplings
    • DOI 10.1021/ja981019t
    • Lesage A, Steuernagel S, Emsley L (1998) Carbon-13 spectral editing in solid-state NMR using heteronuclear scalar couplings. J Am Chem Soc 120:7095-7100 (Pubitemid 28378367)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.28 , pp. 7095-7100
    • Lesage, A.1    Steuernagel, S.2    Emsley, L.3
  • 26
    • 48749091080 scopus 로고    scopus 로고
    • Conformational dynamics of an intact virus: Order parameters for the coat protein of Pf1 bacteriophage
    • 2008PNAS.10510366L 10.1073/pnas.0800405105
    • Lorieau JL, Day LA, McDermott AE (2008) Conformational dynamics of an intact virus: order parameters for the coat protein of Pf1 bacteriophage. Proc Natl Acad Sci USA 105:10366-10371
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10366-10371
    • Lorieau, J.L.1    Day, L.A.2    McDermott, A.E.3
  • 27
    • 0344393786 scopus 로고    scopus 로고
    • High-resolution solid-state NMR applied to polypeptides and membrane proteins
    • 10.1021/ar020232y
    • Luca S, Heise H, Baldus M (2003) High-resolution solid-state NMR applied to polypeptides and membrane proteins. Acc Chem Res 36:858-865
    • (2003) Acc Chem Res , vol.36 , pp. 858-865
    • Luca, S.1    Heise, H.2    Baldus, M.3
  • 28
    • 2442501190 scopus 로고    scopus 로고
    • Separation of aromatic-carbon C-13 NMR signals from di-oxygenated alkyl bands by a chemical-shift-anisotropy filter
    • 10.1016/j.ssnmr.2003.09.003
    • Mao JD, Schmidt-Rohr K (2004) Separation of aromatic-carbon C-13 NMR signals from di-oxygenated alkyl bands by a chemical-shift-anisotropy filter. Solid State Nucl Magn Reson 26:36-45
    • (2004) Solid State Nucl Magn Reson , vol.26 , pp. 36-45
    • Mao, J.D.1    Schmidt-Rohr, K.2
  • 29
    • 23844547603 scopus 로고    scopus 로고
    • 13C NMR by three-spin coherence selection
    • DOI 10.1016/j.jmr.2005.04.016, PII S1090780705001527
    • Mao J-D, Schmidt-Rohr K (2005) Methylene spectral editing in solid-state 13C NMR by three-spin coherence selection. J Magn Reson 176:1-6 (Pubitemid 41162469)
    • (2005) Journal of Magnetic Resonance , vol.176 , Issue.1 , pp. 1-6
    • Mao, J.-D.1    Schmidt-Rohr, K.2
  • 30
    • 34547135200 scopus 로고    scopus 로고
    • Characterization of a nitrogen-rich fulvic acid and its precursor algae from solid state NMR
    • DOI 10.1016/j.orggeochem.2007.04.005, PII S0146638007000976
    • Mao J-D, Cory RM, McKnight DM, Schmidt-Rohr K (2007a) Characterization of a nitrogen-rich fulvic acid and its precursor algae by solid-state NMR. Org Geochem 38:1277-1292 (Pubitemid 47102427)
    • (2007) Organic Geochemistry , vol.38 , Issue.8 , pp. 1277-1292
    • Mao, J.1    Cory, R.M.2    McKnight, D.M.3    Schmidt-Rohr, K.4
  • 31
    • 35648935844 scopus 로고    scopus 로고
    • Humic acids from particulate organic matter in the Saguenay Fjord and the St. Lawrence Estuary investigated by advanced solid-state NMR
    • DOI 10.1016/j.gca.2007.09.022, PII S0016703707005339
    • Mao J-D, Tremblay L, Gagné J-P, Kohl S, Rice J, Schmidt-Rohr K (2007b) Natural organic matter in the Saguenay Fjord and the St. Lawrence Estuary investigated by advanced solid-state NMR. Geochim Cosmochim Acta 71:5483-5499 (Pubitemid 350028610)
    • (2007) Geochimica et Cosmochimica Acta , vol.71 , Issue.22 , pp. 5483-5499
    • Mao, J.-D.1    Tremblay, L.2    Gagne, J.-P.3    Kohl, S.4    Rice, J.5    Schmidt-Rohr, K.6
  • 32
    • 0042995329 scopus 로고    scopus 로고
    • Chemical shift referencing in MAS solid state NMR
    • 2003JMagR.162.479M 10.1016/S1090-7807(03)00082-X
    • Morcombe CR, Zilm KW (2003) Chemical shift referencing in MAS solid state NMR. J Magn Reson 162:479-486
    • (2003) J Magn Reson , vol.162 , pp. 479-486
    • Morcombe, C.R.1    Zilm, K.W.2
  • 33
    • 0035795429 scopus 로고    scopus 로고
    • 15N signal assignments of the α-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 tesla
    • Pauli J, Baldus M, vanRossum B, Groot Hd, Oschkinat H (2001) Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic-angle spinning solid-state NMR at 17.6 Tesla. ChemBioChem 2:272-281 (Pubitemid 33722556)
    • (2001) ChemBioChem , vol.2 , Issue.4 , pp. 272-281
    • Pauli, J.1    Baldus, M.2    Van Rossum, B.3    De Groot, H.4    Oschkinat, H.5
  • 34
    • 81855172000 scopus 로고    scopus 로고
    • Dynamic nuclear polarization-enhanced solid-state NMR of a 13C-labeled signal peptide bound to lipid-reconstituted Sec translocon
    • 10.1021/ja209378h
    • Reggie L, Lopez JJ, Collinson I, Glaubitz C, Lorch M (2011) Dynamic nuclear polarization-enhanced solid-state NMR of a 13C-labeled signal peptide bound to lipid-reconstituted Sec translocon. J Am Chem Soc 133:19084-19086
    • (2011) J Am Chem Soc , vol.133 , pp. 19084-19086
    • Reggie, L.1    Lopez, J.J.2    Collinson, I.3    Glaubitz, C.4    Lorch, M.5
  • 35
    • 0035743666 scopus 로고    scopus 로고
    • Spectral editing in solid-state NMR using scalar multiple quantum filters
    • 2001JMagR.151.40S 10.1006/jmre.2001.2338
    • Sakellariou D, Lesage A, Emsley L (2001) Spectral editing in solid-state NMR using scalar multiple quantum filters. J Magn Reson 151:40-47
    • (2001) J Magn Reson , vol.151 , pp. 40-47
    • Sakellariou, D.1    Lesage, A.2    Emsley, L.3
  • 36
    • 0037182956 scopus 로고    scopus 로고
    • Selective observation of nitrogen-bonded carbons in solid-state NMR by saturation-pulse induced dipolar exchange with recoupling
    • 2002CPL.359.403S 10.1016/S0009-2614(02)00740-6
    • Schmidt-Rohr K, Mao J-D (2002a) Selective observation of nitrogen-bonded carbons in solid-state NMR by saturation-pulse induced dipolar exchange with recoupling. Chem Phys Lett 359:403-411
    • (2002) Chem Phys Lett , vol.359 , pp. 403-411
    • Schmidt-Rohr, K.1    Mao, J.-D.2
  • 37
    • 0037146078 scopus 로고    scopus 로고
    • 1H chemical-shift filtering
    • DOI 10.1021/ja027362m
    • Schmidt-Rohr K, Mao JD (2002b) Efficient CH-group selection and identification in C-13 solid-state NMR by dipolar DEPT and H-1 chemical-shift filtering. J Am Chem Soc 124:13938-13948 (Pubitemid 35379008)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.46 , pp. 13938-13948
    • Schmidt-Rohr, K.1    Mao, J.-D.2
  • 40
    • 2342590696 scopus 로고    scopus 로고
    • Compensation for pulse imperfections in rotational-echo double-resonance NMR by composite pulses and EXORCYCLE
    • 2004JMagR.168.358S 10.1016/j.jmr.2004.03.025
    • Sinha N, Schmidt-Rohr K, Hong H (2004) Compensation for pulse imperfections in rotational-echo double-resonance NMR by composite pulses and EXORCYCLE. J Magn Reson 168:358-365
    • (2004) J Magn Reson , vol.168 , pp. 358-365
    • Sinha, N.1    Schmidt-Rohr, K.2    Hong, H.3
  • 41
    • 80052553690 scopus 로고    scopus 로고
    • Conformational disorder of membrane peptides investigated from solid-state NMR linewidths and lineshapes
    • 10.1021/jp205002n
    • Su Y, Hong M (2011) Conformational disorder of membrane peptides investigated from solid-state NMR linewidths and lineshapes. J Phys Chem B 115:10758-10767
    • (2011) J Phys Chem B , vol.115 , pp. 10758-10767
    • Su, Y.1    Hong, M.2
  • 42
    • 0000953276 scopus 로고    scopus 로고
    • 1H dipolar-assisted rotational resonance in magic-angle spinning NMR
    • DOI 10.1016/S0009-2614(01)00791-6, PII S0009261401007916
    • Takegoshi K, Nakamura S, Terao T (2001) C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR. Chem Phys Lett 344:631-637 (Pubitemid 33628408)
    • (2001) Chemical Physics Letters , vol.344 , Issue.5-6 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 43
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fibril structure
    • 2011ARPC.62.279T 10.1146/annurev-physchem-032210-103539
    • Tycko R (2011) Solid-state NMR studies of amyloid fibril structure. Annu Rev Phys Chem 62:279-299
    • (2011) Annu Rev Phys Chem , vol.62 , pp. 279-299
    • Tycko, R.1
  • 44
    • 4244132605 scopus 로고
    • Measurement of nuclear magnetic dipole-dipole couplings in magic angle spinning NMR
    • 1990CPL.173.461T 10.1016/0009-2614(90)87235-J
    • Tycko R, Dabbagh G (1990) Measurement of nuclear magnetic dipole-dipole couplings in magic angle spinning NMR. Chem Phys Lett 173:461-465
    • (1990) Chem Phys Lett , vol.173 , pp. 461-465
    • Tycko, R.1    Dabbagh, G.2
  • 45
    • 30844458347 scopus 로고    scopus 로고
    • SPINEVOLUTION: A powerful tool for the simulation of solid and liquid state NMR experiments
    • DOI 10.1016/j.jmr.2005.07.018, PII S1090780705002442
    • Veshtort M, Griffin RG (2006) SPINEVOLUTION: a powerful tool for the simulation of solid and liquid state NMR experiments. J Magn Reson 178:248-282 (Pubitemid 43107933)
    • (2006) Journal of Magnetic Resonance , vol.178 , Issue.2 , pp. 248-282
    • Veshtort, M.1    Griffin, R.G.2
  • 46
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • 10.1021/bi00121a010
    • Wishart DS, Sykes BD, Richards FM (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31:1647-1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 47
    • 0000563331 scopus 로고
    • Spectral editing in CPMAS NMR. Generating subspectra based on proton multiplicities
    • 10.1006/jmra.1993.1092
    • Wu XL, Zilm KW (1993) Spectral editing in CPMAS NMR. Generating subspectra based on proton multiplicities. J Magn Reson A 102:205-213
    • (1993) J Magn Reson A , vol.102 , pp. 205-213
    • Wu, X.L.1    Zilm, K.W.2
  • 48
    • 43949157887 scopus 로고
    • Complete spectral editing in CPMAS NMR
    • 10.1006/jmra.1994.1222
    • Wu X-L, Burns ST, Zilm KW (1994) Complete spectral editing in CPMAS NMR. J Magn Reson A 111:29-36
    • (1994) J Magn Reson A , vol.111 , pp. 29-36
    • Wu, X.-L.1    Burns, S.T.2    Zilm, K.W.3


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