메뉴 건너뛰기




Volumn 385, Issue 4, 2009, Pages 1127-1141

Structure of Amantadine-Bound M2 Transmembrane Peptide of Influenza A in Lipid Bilayers from Magic-Angle-Spinning Solid-State NMR: The Role of Ser31 in Amantadine Binding

Author keywords

amantadine; chemical shifts; influenza M2 proton channel; magic angle spinning; solid state NMR

Indexed keywords

AMANTADINE; GLYCINE; MEMBRANE PROTEIN; MONOMER; PROTEIN M2; SERINE; TRYPTOPHAN; VIRUS PROTEIN;

EID: 58149345493     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.11.022     Document Type: Article
Times cited : (137)

References (56)
  • 1
    • 33845543992 scopus 로고    scopus 로고
    • Controlling influenza virus replication by inhibiting its proton channel
    • Pinto L.H., and Lamb R.A. Controlling influenza virus replication by inhibiting its proton channel. Mol. Biosyst. 3 (2007) 18-23
    • (2007) Mol. Biosyst. , vol.3 , pp. 18-23
    • Pinto, L.H.1    Lamb, R.A.2
  • 2
    • 25844438380 scopus 로고    scopus 로고
    • Incidence of adamantane resistance among influenza A (H3N2) viruses isolated worldwide from 1994 to 2005: a cause for concern
    • Bright R.A., Medina M.J., Xu X., Perez-Oronoz G., Wallis T.R., Davis X.M., et al. Incidence of adamantane resistance among influenza A (H3N2) viruses isolated worldwide from 1994 to 2005: a cause for concern. Lancet 366 (2005) 1175-1181
    • (2005) Lancet , vol.366 , pp. 1175-1181
    • Bright, R.A.1    Medina, M.J.2    Xu, X.3    Perez-Oronoz, G.4    Wallis, T.R.5    Davis, X.M.6
  • 3
    • 0003156040 scopus 로고
    • The influenza A virus M2 ion channel protein and its role in the influenza virus life cycle
    • Wemmer E. (Ed), Cold Spring Harbor Lab Press, Plainview, NY
    • Lamb R.A., Holsinger K.J., and Pinto L.H. The influenza A virus M2 ion channel protein and its role in the influenza virus life cycle. In: Wemmer E. (Ed). Cellular receptors of animal viruses (1994), Cold Spring Harbor Lab Press, Plainview, NY 303-321
    • (1994) Cellular receptors of animal viruses , pp. 303-321
    • Lamb, R.A.1    Holsinger, K.J.2    Pinto, L.H.3
  • 4
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto L.H., Holsinger L.J., and Lamb R.A. Influenza virus M2 protein has ion channel activity. Cell 69 (1992) 517-528
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 5
    • 0028181687 scopus 로고
    • Influenza A virus M2 ion channel protein: a structure-function analysis
    • Holsinger L.J., Nichani D., Pinto L.H., and Lamb R.A. Influenza A virus M2 ion channel protein: a structure-function analysis. J. Virol. 68 (1994) 1551-1563
    • (1994) J. Virol. , vol.68 , pp. 1551-1563
    • Holsinger, L.J.1    Nichani, D.2    Pinto, L.H.3    Lamb, R.A.4
  • 6
    • 0030973121 scopus 로고    scopus 로고
    • The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer
    • Sakaguchi T., Tu Q., Pinto L.H., and Lamb R.A. The active oligomeric state of the minimalistic influenza virus M2 ion channel is a tetramer. Proc. Natl Acad. Sci. USA 94 (1997) 5000-5005
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5000-5005
    • Sakaguchi, T.1    Tu, Q.2    Pinto, L.H.3    Lamb, R.A.4
  • 7
    • 40349105892 scopus 로고    scopus 로고
    • Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel
    • Cady S.D., and Hong M. Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel. Proc. Natl Acad. Sci. USA 105 (2008) 1483-1488
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 1483-1488
    • Cady, S.D.1    Hong, M.2
  • 8
    • 33646494326 scopus 로고    scopus 로고
    • Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity
    • Hu J., Fu R., Nishimura K., Zhang L., Zhou H.X., Busath D.D., et al. Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity. Proc. Natl Acad. Sci. USA 103 (2006) 6865-6870
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 6865-6870
    • Hu, J.1    Fu, R.2    Nishimura, K.3    Zhang, L.4    Zhou, H.X.5    Busath, D.D.6
  • 9
    • 0037131381 scopus 로고    scopus 로고
    • The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue
    • Tang Y., Zaitseva F., Lamb R.A., and Pinto L.H. The gate of the influenza virus M2 proton channel is formed by a single tryptophan residue. J. Biol. Chem. 277 (2002) 39880-39886
    • (2002) J. Biol. Chem. , vol.277 , pp. 39880-39886
    • Tang, Y.1    Zaitseva, F.2    Lamb, R.A.3    Pinto, L.H.4
  • 10
    • 0026785994 scopus 로고
    • The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers
    • Duff K.C., and Ashley R.H. The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers. Virology 190 (1992) 485-489
    • (1992) Virology , vol.190 , pp. 485-489
    • Duff, K.C.1    Ashley, R.H.2
  • 11
    • 0030881872 scopus 로고    scopus 로고
    • A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity
    • Pinto L.H., Dieckmann G.R., Gandhi C.S., Papworth C.G., Braman J., Shaughnessy M.A., et al. A functionally defined model for the M2 proton channel of influenza A virus suggests a mechanism for its ion selectivity. Proc. Natl Acad. Sci. USA 94 (1997) 11301-11306
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11301-11306
    • Pinto, L.H.1    Dieckmann, G.R.2    Gandhi, C.S.3    Papworth, C.G.4    Braman, J.5    Shaughnessy, M.A.6
  • 12
    • 0033554426 scopus 로고    scopus 로고
    • Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly
    • Kochendoerfer G.G., Salom D., Lear J.D., Wilk-Orescan R., Kent S.B., and DeGrado W.F. Total chemical synthesis of the integral membrane protein influenza A virus M2: role of its C-terminal domain in tetramer assembly. Biochemistry 38 (1999) 11905-11913
    • (1999) Biochemistry , vol.38 , pp. 11905-11913
    • Kochendoerfer, G.G.1    Salom, D.2    Lear, J.D.3    Wilk-Orescan, R.4    Kent, S.B.5    DeGrado, W.F.6
  • 13
    • 52249123874 scopus 로고    scopus 로고
    • pH-induced conformational change of the influenza M2 protein C-terminal domain
    • Nguyen P.A., Soto C.S., Polishchuk A., Caputo G.A., Tatko C.D., Ma C., et al. pH-induced conformational change of the influenza M2 protein C-terminal domain. Biochemistry 47 (2008) 9934-9936
    • (2008) Biochemistry , vol.47 , pp. 9934-9936
    • Nguyen, P.A.1    Soto, C.S.2    Polishchuk, A.3    Caputo, G.A.4    Tatko, C.D.5    Ma, C.6
  • 14
    • 38749106195 scopus 로고    scopus 로고
    • Structure and mechanism of the M2 proton channel of influenza A virus
    • Schnell J.R., and Chou J.J. Structure and mechanism of the M2 proton channel of influenza A virus. Nature 451 (2008) 591-595
    • (2008) Nature , vol.451 , pp. 591-595
    • Schnell, J.R.1    Chou, J.J.2
  • 15
    • 38749151911 scopus 로고    scopus 로고
    • Structural basis for the function and inhibition of an influenza virus proton channel
    • Stouffer A.L., Acharya R., Salom D., Levine A.S., Di Costanzo L., Soto C.S., et al. Structural basis for the function and inhibition of an influenza virus proton channel. Nature 451 (2008) 596-599
    • (2008) Nature , vol.451 , pp. 596-599
    • Stouffer, A.L.1    Acharya, R.2    Salom, D.3    Levine, A.S.4    Di Costanzo, L.5    Soto, C.S.6
  • 16
    • 38749099067 scopus 로고    scopus 로고
    • Ion channels: coughing up flu's proton channels
    • Miller C. Ion channels: coughing up flu's proton channels. Nature 451 (2008) 532-533
    • (2008) Nature , vol.451 , pp. 532-533
    • Miller, C.1
  • 17
    • 0037139592 scopus 로고    scopus 로고
    • Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel
    • Chou J.J., Kaufman J.D., Stahl S.J., Wingfield P.T., and Bax A. Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel. J. Am. Chem. Soc. 124 (2002) 2450-2451
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2450-2451
    • Chou, J.J.1    Kaufman, J.D.2    Stahl, S.J.3    Wingfield, P.T.4    Bax, A.5
  • 18
    • 34250334756 scopus 로고    scopus 로고
    • Backbone structure of the amantadine-block trans-membrane domain M2 proton channel from influenza A virus
    • Hu J., Asbury T., Achuthan S., Li C., Bertram R., Quine J.R., et al. Backbone structure of the amantadine-block trans-membrane domain M2 proton channel from influenza A virus. Biophys. J. 92 (2007) 4335-4343
    • (2007) Biophys. J. , vol.92 , pp. 4335-4343
    • Hu, J.1    Asbury, T.2    Achuthan, S.3    Li, C.4    Bertram, R.5    Quine, J.R.6
  • 19
    • 0034775070 scopus 로고    scopus 로고
    • Structure of the transmembrane region of the M2 protein H(+) channel
    • Wang J., Kim S., Kovacs F., and Cross T.A. Structure of the transmembrane region of the M2 protein H(+) channel. Protein Sci. 10 (2001) 2241-2250
    • (2001) Protein Sci. , vol.10 , pp. 2241-2250
    • Wang, J.1    Kim, S.2    Kovacs, F.3    Cross, T.A.4
  • 20
    • 34247847729 scopus 로고    scopus 로고
    • 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle
    • 15N solid-state NMR investigation of the dynamics and orientation of a transmembrane helical bundle. J. Am. Chem. Soc. 129 (2007) 5719-5729
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5719-5729
    • Cady, S.D.1    Goodman, C.2    Tatko, C.D.3    DeGrado, W.F.4    Hong, M.5
  • 21
    • 40949146901 scopus 로고    scopus 로고
    • 13C-detected N-H dipolar couplings under magic angle spinning
    • 13C-detected N-H dipolar couplings under magic angle spinning. J. Magn. Reson. 191 (2008) 219-225
    • (2008) J. Magn. Reson. , vol.191 , pp. 219-225
    • Cady, S.D.1    Hong, M.2
  • 22
    • 33744941313 scopus 로고    scopus 로고
    • Determination of the oligomeric number and intermolecular distances of membrane protein assemblies by anisotropic (1)H-driven spin diffusion NMR spectroscopy
    • Luo W., and Hong M. Determination of the oligomeric number and intermolecular distances of membrane protein assemblies by anisotropic (1)H-driven spin diffusion NMR spectroscopy. J. Am. Chem. Soc. 128 (2006) 7242-7251
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 7242-7251
    • Luo, W.1    Hong, M.2
  • 23
    • 34848868442 scopus 로고    scopus 로고
    • Side chain conformation and gating of the M2 transmembrane peptide proton channel of influenza A virus from solid-state NMR
    • Luo W., Mani R., and Hong M. Side chain conformation and gating of the M2 transmembrane peptide proton channel of influenza A virus from solid-state NMR. J. Phys. Chem. 111 (2007) 10825-10832
    • (2007) J. Phys. Chem. , vol.111 , pp. 10825-10832
    • Luo, W.1    Mani, R.2    Hong, M.3
  • 24
    • 0027339698 scopus 로고
    • Influenza virus M2 protein: a molecular modelling study of the ion channel
    • Sansom M.S., and Kerr I.D. Influenza virus M2 protein: a molecular modelling study of the ion channel. Protein Eng. 6 (1993) 65-74
    • (1993) Protein Eng. , vol.6 , pp. 65-74
    • Sansom, M.S.1    Kerr, I.D.2
  • 25
    • 0027963402 scopus 로고
    • Neutron diffraction reveals the site of amantadine blockade in the influenza A M2 ion channel
    • Duff K.C., Gilchrist P.J., Saxena A.M., and Bradshaw J.P. Neutron diffraction reveals the site of amantadine blockade in the influenza A M2 ion channel. Virology 202 (1994) 287-293
    • (1994) Virology , vol.202 , pp. 287-293
    • Duff, K.C.1    Gilchrist, P.J.2    Saxena, A.M.3    Bradshaw, J.P.4
  • 26
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G., Delaglio F., and Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13 (1999) 289-302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 27
    • 0028188303 scopus 로고
    • Chemical shifts of carbonyl carbons in peptides and proteins
    • de Dios A.C., and Oldfield E. Chemical shifts of carbonyl carbons in peptides and proteins. J. Am. Chem. Soc. 116 (1994) 11485-11488
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 11485-11488
    • de Dios, A.C.1    Oldfield, E.2
  • 28
    • 4744352080 scopus 로고    scopus 로고
    • Amantadine partition and localization in phospholipid membrane: a solution NMR study
    • Wang J., Schnell J.R., and Chou J.J. Amantadine partition and localization in phospholipid membrane: a solution NMR study. Biochem. Biophys. Res. Commun. 324 (2004) 212-217
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 212-217
    • Wang, J.1    Schnell, J.R.2    Chou, J.J.3
  • 29
    • 38949181061 scopus 로고    scopus 로고
    • Solid-state NMR and MD simulations of the antiviral drug amantadine solubilized in DMPC bilayers
    • Li C., Yi M., Hu J., Zhou H.X., and Cross T.A. Solid-state NMR and MD simulations of the antiviral drug amantadine solubilized in DMPC bilayers. Biophys. J. 94 (2008) 1295-1302
    • (2008) Biophys. J. , vol.94 , pp. 1295-1302
    • Li, C.1    Yi, M.2    Hu, J.3    Zhou, H.X.4    Cross, T.A.5
  • 30
    • 0031669384 scopus 로고    scopus 로고
    • Partitioning and localization of spin-labeled amantadine in lipid bilayers: an EPR study
    • Subczynski W.K., Wojas J., Pezeshk V., and Pezeshk A. Partitioning and localization of spin-labeled amantadine in lipid bilayers: an EPR study. J. Pharm. Sci. 87 (1998) 1249-1254
    • (1998) J. Pharm. Sci. , vol.87 , pp. 1249-1254
    • Subczynski, W.K.1    Wojas, J.2    Pezeshk, V.3    Pezeshk, A.4
  • 31
    • 36849047240 scopus 로고    scopus 로고
    • Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel
    • Li C., Qin H., Gao F.P., and Cross T.A. Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel. Biochim. Biophys. Acta 1768 (2007) 3162-3170
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3162-3170
    • Li, C.1    Qin, H.2    Gao, F.P.3    Cross, T.A.4
  • 32
    • 0025222978 scopus 로고
    • A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids
    • O'Neil K.T., and DeGrado W.F. A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250 (1990) 646-651
    • (1990) Science , vol.250 , pp. 646-651
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 33
    • 0032817780 scopus 로고    scopus 로고
    • Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association
    • Javadpour M.M., Eilers M., Groesbeek M., and Smith S.O. Helix packing in polytopic membrane proteins: role of glycine in transmembrane helix association. Biophys. J. 77 (1999) 1609-1618
    • (1999) Biophys. J. , vol.77 , pp. 1609-1618
    • Javadpour, M.M.1    Eilers, M.2    Groesbeek, M.3    Smith, S.O.4
  • 34
    • 0037172965 scopus 로고    scopus 로고
    • Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein
    • Howard K.P., Lear J.D., and DeGrado W.F. Sequence determinants of the energetics of folding of a transmembrane four-helix-bundle protein. Proc. Natl Acad. Sci. USA 99 (2002) 8568-8572
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8568-8572
    • Howard, K.P.1    Lear, J.D.2    DeGrado, W.F.3
  • 35
    • 16244391442 scopus 로고    scopus 로고
    • Determination of peptide oligomerization in lipid membranes with magic-angle spinning spin diffusion NMR
    • Buffy J.J., Waring A.J., and Hong M. Determination of peptide oligomerization in lipid membranes with magic-angle spinning spin diffusion NMR. J. Am. Chem. Soc. 127 (2005) 4477-4483
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4477-4483
    • Buffy, J.J.1    Waring, A.J.2    Hong, M.3
  • 36
    • 0028280706 scopus 로고
    • Four helix bundle diversity in globular proteins
    • Harris N.L., Presnell S.R., and Cohen F.E. Four helix bundle diversity in globular proteins. J. Mol. Biol. 236 (1994) 1356-1368
    • (1994) J. Mol. Biol. , vol.236 , pp. 1356-1368
    • Harris, N.L.1    Presnell, S.R.2    Cohen, F.E.3
  • 37
    • 15244348542 scopus 로고    scopus 로고
    • The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment
    • Duong-Ly K.C., Nanda V., DeGrado W.F., and Howard K.P. The conformation of the pore region of the M2 proton channel depends on lipid bilayer environment. Protein Sci. 14 (2005) 856-861
    • (2005) Protein Sci. , vol.14 , pp. 856-861
    • Duong-Ly, K.C.1    Nanda, V.2    DeGrado, W.F.3    Howard, K.P.4
  • 39
    • 0028434564 scopus 로고
    • 15N NMR chemical shifts in proteins and secondary structure
    • 15N NMR chemical shifts in proteins and secondary structure. J. Biomol. NMR 4 (1994) 341-348
    • (1994) J. Biomol. NMR , vol.4 , pp. 341-348
    • Le, H.1    Oldfield, E.2
  • 40
    • 0027308278 scopus 로고
    • Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach
    • deDios A.C., Pearson J.G., and Oldfield E. Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach. Science 260 (1993) 1491-1496
    • (1993) Science , vol.260 , pp. 1491-1496
    • deDios, A.C.1    Pearson, J.G.2    Oldfield, E.3
  • 41
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: a database of uniformly referenced protein chemical shifts
    • Zhang H., Neal S., and Wishart D.S. RefDB: a database of uniformly referenced protein chemical shifts. J. Biomol. NMR 25 (2003) 173-195
    • (2003) J. Biomol. NMR , vol.25 , pp. 173-195
    • Zhang, H.1    Neal, S.2    Wishart, D.S.3
  • 42
    • 49449093199 scopus 로고    scopus 로고
    • Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel
    • Jing X., Ma C., Ohigashi Y., Oliveira F.A., Jardetzky T.S., Pinto L.H., and Lamb R.A. Functional studies indicate amantadine binds to the pore of the influenza A virus M2 proton-selective ion channel. Proc. Natl Acad. Sci. USA 105 (2008) 10967-10972
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 10967-10972
    • Jing, X.1    Ma, C.2    Ohigashi, Y.3    Oliveira, F.A.4    Jardetzky, T.S.5    Pinto, L.H.6    Lamb, R.A.7
  • 44
    • 33947091567 scopus 로고
    • 9-Fluorenylmethoxycarbonyl amino-protecting group
    • Carpino L.A., and Han G.Y. 9-Fluorenylmethoxycarbonyl amino-protecting group. J. Org. Chem. 37 (1972) 3404-3409
    • (1972) J. Org. Chem. , vol.37 , pp. 3404-3409
    • Carpino, L.A.1    Han, G.Y.2
  • 45
    • 0026004791 scopus 로고
    • Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins
    • Ito T., Gorman O.T., Kawaoka Y., Bean W.J., and Webster R.G. Evolutionary analysis of the influenza A virus M gene with comparison of the M1 and M2 proteins. J. Virol. 65 (1991) 5491-5498
    • (1991) J. Virol. , vol.65 , pp. 5491-5498
    • Ito, T.1    Gorman, O.T.2    Kawaoka, Y.3    Bean, W.J.4    Webster, R.G.5
  • 48
    • 0033629304 scopus 로고    scopus 로고
    • An improved broadband decoupling sequence for liquid crystals and solids
    • Fung B.M., Khitrin A.K., and Ermolaev K. An improved broadband decoupling sequence for liquid crystals and solids. J. Magn. Reson. 142 (2000) 97-101
    • (2000) J. Magn. Reson. , vol.142 , pp. 97-101
    • Fung, B.M.1    Khitrin, A.K.2    Ermolaev, K.3
  • 49
    • 0000432697 scopus 로고    scopus 로고
    • Fivefold symmetric homonuclear dipolar recoupling in rotating solids: application to double-quantum spectroscopy
    • Hohwy M., Rienstra C.M., Jaroniec C.P., and Griffin R.G. Fivefold symmetric homonuclear dipolar recoupling in rotating solids: application to double-quantum spectroscopy. J. Chem. Phys. 110 (1999) 7983-7992
    • (1999) J. Chem. Phys. , vol.110 , pp. 7983-7992
    • Hohwy, M.1    Rienstra, C.M.2    Jaroniec, C.P.3    Griffin, R.G.4
  • 50
    • 0000953276 scopus 로고    scopus 로고
    • C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR
    • Takegoshi K., Nakamura S., and Terao T. C-13-H-1 dipolar-assisted rotational resonance in magic-angle spinning NMR. Chem. Phys. Lett. 344 (2001) 631-637
    • (2001) Chem. Phys. Lett. , vol.344 , pp. 631-637
    • Takegoshi, K.1    Nakamura, S.2    Terao, T.3
  • 52
    • 0032615011 scopus 로고    scopus 로고
    • Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width
    • Hong M. Solid-state dipolar INADEQUATE NMR spectroscopy with a large double-quantum spectral width. J. Magn. Reson. 136 (1999) 86-91
    • (1999) J. Magn. Reson. , vol.136 , pp. 86-91
    • Hong, M.1
  • 53
    • 45149145322 scopus 로고
    • Rotational echo double resonance NMR
    • Gullion T., and Schaefer J. Rotational echo double resonance NMR. J. Magn. Reson. 81 (1989) 196-200
    • (1989) J. Magn. Reson. , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 55
    • 23844547603 scopus 로고    scopus 로고
    • Methylene spectral editing in solid-state C-13 NMR by three-spin coherence selection
    • Mao J.D., and Schmidt-Rohr K. Methylene spectral editing in solid-state C-13 NMR by three-spin coherence selection. J. Magn. Reson. 176 (2005) 1-6
    • (2005) J. Magn. Reson. , vol.176 , pp. 1-6
    • Mao, J.D.1    Schmidt-Rohr, K.2
  • 56


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.