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Volumn 1768, Issue 12, 2007, Pages 3162-3170

Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel

Author keywords

Conformational plasticity; Influenza A virus; M2 channel; Membrane protein; PISEMA; Solid state NMR

Indexed keywords

AMANTADINE; MEMBRANE PROTEIN; PROTEIN M2; PROTON;

EID: 36849047240     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2007.08.025     Document Type: Article
Times cited : (83)

References (80)
  • 1
    • 0036226583 scopus 로고    scopus 로고
    • Comparison of helix interactions in membrane and soluble α-bundle proteins
    • Eilers M., Patel A.B., Liu W., and Smith S.O. Comparison of helix interactions in membrane and soluble α-bundle proteins. Biophys. J. 82 (2002) 2720-2736
    • (2002) Biophys. J. , vol.82 , pp. 2720-2736
    • Eilers, M.1    Patel, A.B.2    Liu, W.3    Smith, S.O.4
  • 2
    • 23044510444 scopus 로고    scopus 로고
    • Transmembrane helices before, during and after insertion
    • White S.H., and von Heijne G. Transmembrane helices before, during and after insertion. Curr. Opin. Struct. Biol. 15 (2005) 378-386
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 378-386
    • White, S.H.1    von Heijne, G.2
  • 3
    • 85051972100 scopus 로고
    • Determination of the structure of fluid lipid bilayer membranes
    • DiSalvo E.A., and Simon S.A. (Eds), CRC Press, Boca Raton
    • White S.H., and Wiener M.C. Determination of the structure of fluid lipid bilayer membranes. In: DiSalvo E.A., and Simon S.A. (Eds). Permeability and Stability of Lipid Bilayers (1994), CRC Press, Boca Raton 1-19
    • (1994) Permeability and Stability of Lipid Bilayers , pp. 1-19
    • White, S.H.1    Wiener, M.C.2
  • 5
    • 0033028551 scopus 로고    scopus 로고
    • Lipid composition and the lateral pressure profile in bilayers
    • Cantor R.S. Lipid composition and the lateral pressure profile in bilayers. Biophys. J. 76 (1999) 2625-2639
    • (1999) Biophys. J. , vol.76 , pp. 2625-2639
    • Cantor, R.S.1
  • 6
    • 0037150089 scopus 로고    scopus 로고
    • Conformational energetics of rhodopsin modulated by nonlamellar forming lipids
    • Botelho A.V., Gibson N.J., Thurmond R.L., Wang Y., and Brown M.F. Conformational energetics of rhodopsin modulated by nonlamellar forming lipids. Biochemistry 41 (2002) 6354-6368
    • (2002) Biochemistry , vol.41 , pp. 6354-6368
    • Botelho, A.V.1    Gibson, N.J.2    Thurmond, R.L.3    Wang, Y.4    Brown, M.F.5
  • 7
    • 33746358793 scopus 로고    scopus 로고
    • Introduction to the membrane protein reviews: the interplay of structure, dynamics and environment in membrane protein function
    • Sachs J.N., and Engelman D.M. Introduction to the membrane protein reviews: the interplay of structure, dynamics and environment in membrane protein function. Ann. Rev. Biochem. 75 (2006) 707-712
    • (2006) Ann. Rev. Biochem. , vol.75 , pp. 707-712
    • Sachs, J.N.1    Engelman, D.M.2
  • 8
    • 0019464222 scopus 로고
    • The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis
    • Engelman D.M., and Steitz T.A. The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell 23 (1981) 411-422
    • (1981) Cell , vol.23 , pp. 411-422
    • Engelman, D.M.1    Steitz, T.A.2
  • 9
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: the two-stage model
    • Popot J.L., and Engelman D.M. Membrane protein folding and oligomerization: the two-stage model. Biochemistry 29 (1990) 4031-4037
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 10
    • 0030448915 scopus 로고    scopus 로고
    • Crossing the hydrophobic barrier: insertion of membrane proteins
    • Engelman D.M. Crossing the hydrophobic barrier: insertion of membrane proteins. Science 274 (1996) 1850-1851
    • (1996) Science , vol.274 , pp. 1850-1851
    • Engelman, D.M.1
  • 12
    • 0032796426 scopus 로고    scopus 로고
    • Role of hydration water in protein unfolding
    • Robinson G.W., and Cho C.H. Role of hydration water in protein unfolding. Biophys. J. 77 (1999) 3311-3318
    • (1999) Biophys. J. , vol.77 , pp. 3311-3318
    • Robinson, G.W.1    Cho, C.H.2
  • 13
    • 0033064923 scopus 로고    scopus 로고
    • The temperature dependence of integral molecular motions in hydrated and dry α-amylase: the role of hydration water in the dynamical transition of proteins
    • Fitter J. The temperature dependence of integral molecular motions in hydrated and dry α-amylase: the role of hydration water in the dynamical transition of proteins. Biophys. J. 76 (1999) 1034-1042
    • (1999) Biophys. J. , vol.76 , pp. 1034-1042
    • Fitter, J.1
  • 14
    • 0033529783 scopus 로고    scopus 로고
    • Water: a "foldase" that catalyzes hydrogen bond exchange in polypeptide conformational rearrangements
    • Xu F., and Cross T.A. Water: a "foldase" that catalyzes hydrogen bond exchange in polypeptide conformational rearrangements. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 9057-9061
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9057-9061
    • Xu, F.1    Cross, T.A.2
  • 15
    • 1542358793 scopus 로고    scopus 로고
    • De novo folding of membrane proteins: an exploration of the structure and NMR properties of the FD coat protein
    • Im W., and Brooks III C.L. De novo folding of membrane proteins: an exploration of the structure and NMR properties of the FD coat protein. J. Mol. Biol. 337 (2004) 513-519
    • (2004) J. Mol. Biol. , vol.337 , pp. 513-519
    • Im, W.1    Brooks III, C.L.2
  • 16
    • 18744403982 scopus 로고    scopus 로고
    • Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations
    • Im W., and Brooks III C.L. Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 6771-6776
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6771-6776
    • Im, W.1    Brooks III, C.L.2
  • 18
    • 0032480817 scopus 로고    scopus 로고
    • Fourier transform infrared analysis of purified lactose permease: a monodisperse lactose permease preparation is stably folded, α-helical, and highly accessible to deuterium exchange
    • Patzlaff J.S., Moeller J.A., Barry B.A., and Brooker R.J. Fourier transform infrared analysis of purified lactose permease: a monodisperse lactose permease preparation is stably folded, α-helical, and highly accessible to deuterium exchange. Biochemistry 37 (1998) 15363-15375
    • (1998) Biochemistry , vol.37 , pp. 15363-15375
    • Patzlaff, J.S.1    Moeller, J.A.2    Barry, B.A.3    Brooker, R.J.4
  • 19
    • 0142210121 scopus 로고    scopus 로고
    • Initial structure and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers
    • Tian C., Gao F.P., Pinto L.H., Lamb R.A., and Cross T.A. Initial structure and dynamic characterization of the M2 protein transmembrane and amphipathic helices in lipid bilayers. Protein Sci. 12 (2003) 2597-2605
    • (2003) Protein Sci. , vol.12 , pp. 2597-2605
    • Tian, C.1    Gao, F.P.2    Pinto, L.H.3    Lamb, R.A.4    Cross, T.A.5
  • 22
    • 36849043475 scopus 로고    scopus 로고
    • R. Page, C. Li, J. Hu, F.P. Gao, T.A. Cross, Lipid bilayers: an essential environment for the understanding of membrane proteins, Magn. Reson. Chem. (in press).
  • 23
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution-a 60 year old hypothesis revisited
    • James L.C., and Tawfik D.S. Conformational diversity and protein evolution-a 60 year old hypothesis revisited. TRENDS Biochem. Sci. 28 (2003) 361-368
    • (2003) TRENDS Biochem. Sci. , vol.28 , pp. 361-368
    • James, L.C.1    Tawfik, D.S.2
  • 24
    • 27744443715 scopus 로고    scopus 로고
    • Plasticity of acetylcholine receptor gating motions via rate-energy relationships
    • Mitra A., Tascione R., Auerbach A., and Licht S. Plasticity of acetylcholine receptor gating motions via rate-energy relationships. Biophys. J. 89 (2005) 3071-3078
    • (2005) Biophys. J. , vol.89 , pp. 3071-3078
    • Mitra, A.1    Tascione, R.2    Auerbach, A.3    Licht, S.4
  • 25
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., and Chan H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4 (1997) 10-19
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 27
    • 0036086351 scopus 로고    scopus 로고
    • The α-helix and the organization and gating of channels
    • Spencer R.H., and Rees D.C. The α-helix and the organization and gating of channels. Annu. Rev. Biophys. Biomol. Struct. 31 (2002) 207-233
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 207-233
    • Spencer, R.H.1    Rees, D.C.2
  • 29
    • 0025923280 scopus 로고
    • Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds
    • Holsinger L.J., and Lamb R.A. Influenza virus M2 integral membrane protein is a homotetramer stabilized by formation of disulfide bonds. Virology 183 (1991) 32-43
    • (1991) Virology , vol.183 , pp. 32-43
    • Holsinger, L.J.1    Lamb, R.A.2
  • 30
    • 0026008031 scopus 로고
    • Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel
    • Sugrue R.J., and Hay A.J. Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel. Virology 180 (1991) 617-624
    • (1991) Virology , vol.180 , pp. 617-624
    • Sugrue, R.J.1    Hay, A.J.2
  • 31
    • 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. U. S. A. 94 (1997) 5000-5005
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 5000-5005
    • Sakaguchi, T.1    Tu, Q.2    Pinto, L.H.3    Lamb, R.A.4
  • 32
    • 0029816765 scopus 로고    scopus 로고
    • Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells
    • Chizhmakov I.V., Geraghty F.M., Ogden D.C., Hayhurst A., Antoniou N., and Hay A.J. Selective proton permeability and pH regulation of the influenza virus M2 channel expressed in mouse erythroleukaemia cells. J. Physiol. 494 Pt 2 (1996) 329-336
    • (1996) J. Physiol. , vol.494 , Issue.PART 2 , pp. 329-336
    • Chizhmakov, I.V.1    Geraghty, F.M.2    Ogden, D.C.3    Hayhurst, A.4    Antoniou, N.5    Hay, A.J.6
  • 33
    • 0030061323 scopus 로고    scopus 로고
    • Ion selectivity and activation of the M2 ion channel of influenza virus.
    • Shimbo K., Brassard D.L., Lamb R.A., and Pinto L.H. Ion selectivity and activation of the M2 ion channel of influenza virus. Biophys. J. 70 (1996) 1335-1346
    • (1996) Biophys. J. , vol.70 , pp. 1335-1346
    • Shimbo, K.1    Brassard, D.L.2    Lamb, R.A.3    Pinto, L.H.4
  • 36
    • 0022157043 scopus 로고
    • The molecular basis of the specific anti-influenza action of amantadine
    • Hay A.J., Wolstenholme A.J., Skehel J.J., and Smith M.H. The molecular basis of the specific anti-influenza action of amantadine. EMBO J. 4 (1985) 3021-3024
    • (1985) EMBO J. , vol.4 , pp. 3021-3024
    • Hay, A.J.1    Wolstenholme, A.J.2    Skehel, J.J.3    Smith, M.H.4
  • 37
    • 0002988267 scopus 로고
    • The action of adamantamines against influenza A viruses: inhibition of the M2 ion channel protein
    • Hay A.J. The action of adamantamines against influenza A viruses: inhibition of the M2 ion channel protein. Semin. Virol. 3 (1992) 21-30
    • (1992) Semin. Virol. , vol.3 , pp. 21-30
    • Hay, A.J.1
  • 38
    • 0027185716 scopus 로고
    • Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block
    • Wang C., Takeuchi K., Pinto L.H., and Lamb R.A. Ion channel activity of influenza A virus M2 protein: characterization of the amantadine block. J. Virol. 67 (1993) 5585-5594
    • (1993) J. Virol. , vol.67 , pp. 5585-5594
    • Wang, C.1    Takeuchi, K.2    Pinto, L.H.3    Lamb, R.A.4
  • 39
    • 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
  • 40
    • 34250334756 scopus 로고    scopus 로고
    • Backbone structure of the amantadine-blocked transmembrane domain M2 proton channel from influenza A virus
    • Hu J., Asbury T., Achuthan S., Li C., Bertram R., Quine J.R., Fu R., and Cross T.A. Backbone structure of the amantadine-blocked transmembrane 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    Fu, R.7    Cross, T.A.8
  • 42
    • 33744941313 scopus 로고    scopus 로고
    • 1H driven spin diffusion NMR spectroscopy
    • 1H 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
  • 44
    • 0037027306 scopus 로고    scopus 로고
    • + channel helical bundle: combining precise orientational and distance restraints from solid state NMR
    • + channel helical bundle: combining precise orientational and distance restraints from solid state NMR. Biochemistry 41 (2002) 13170-13177
    • (2002) Biochemistry , vol.41 , pp. 13170-13177
    • Nishimura, K.1    Kim, S.2    Zhang, L.3    Cross, T.A.4
  • 45
    • 0033073762 scopus 로고    scopus 로고
    • The influenza virus M2 ion channel protein: probing the structure of the t domain in intact cells by using engineered disulfide cross-linking
    • Bauer C.M., Pinto L.H., Cross T.A., and Lamb R.A. The influenza virus M2 ion channel protein: probing the structure of the t domain in intact cells by using engineered disulfide cross-linking. Virology 254 (1999) 196-209
    • (1999) Virology , vol.254 , pp. 196-209
    • Bauer, C.M.1    Pinto, L.H.2    Cross, T.A.3    Lamb, R.A.4
  • 46
    • 0034700255 scopus 로고    scopus 로고
    • pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus
    • Salom D., Hill B.R., Lear J.D., and DeGrado W.F. pH-dependent tetramerization and amantadine binding of the transmembrane helix of M2 from the influenza A virus. Biochemistry 39 (2000) 14160-14170
    • (2000) Biochemistry , vol.39 , pp. 14160-14170
    • Salom, D.1    Hill, B.R.2    Lear, J.D.3    DeGrado, W.F.4
  • 48
    • 0032992048 scopus 로고    scopus 로고
    • Defining the transmembrane helix of M2 protein from influenza A by molecular dynamics simulations in a lipid bilayer
    • Forrest L.R., Tieleman D.P., and Sansom M.S.P. Defining the transmembrane helix of M2 protein from influenza A by molecular dynamics simulations in a lipid bilayer. Biophys. J. 76 (1999) 1886-1896
    • (1999) Biophys. J. , vol.76 , pp. 1886-1896
    • Forrest, L.R.1    Tieleman, D.P.2    Sansom, M.S.P.3
  • 49
    • 33846804141 scopus 로고    scopus 로고
    • Membrane assembly of simple helix homo-oligomers studied via molecular dynamics simulations
    • Bu L., Im W., and Brooks III C.L. Membrane assembly of simple helix homo-oligomers studied via molecular dynamics simulations. Biophys. J. 92 (2007) 854-863
    • (2007) Biophys. J. , vol.92 , pp. 854-863
    • Bu, L.1    Im, W.2    Brooks III, C.L.3
  • 50
    • 25844476272 scopus 로고    scopus 로고
    • A computational study of the closed and open states of the influenza A M2 proton channel
    • Wu Y., and Voth G.A. A computational study of the closed and open states of the influenza A M2 proton channel. Biophys. J. 89 (2005) 2402-2411
    • (2005) Biophys. J. , vol.89 , pp. 2402-2411
    • Wu, Y.1    Voth, G.A.2
  • 51
    • 28844493428 scopus 로고    scopus 로고
    • + channel: the gating mechanism of influenza A M2
    • + channel: the gating mechanism of influenza A M2. Structure 13 (2005) 1789-1798
    • (2005) Structure , vol.13 , pp. 1789-1798
    • Kass, I.1    Arkin, I.T.2
  • 53
    • 4344704702 scopus 로고    scopus 로고
    • Structure determination of membrane proteins by NMR spectroscopy
    • Opella S.J., and Marassi F.M. Structure determination of membrane proteins by NMR spectroscopy. Chem. Rev. 104 (2004) 3587-3606
    • (2004) Chem. Rev. , vol.104 , pp. 3587-3606
    • Opella, S.J.1    Marassi, F.M.2
  • 55
    • 34247844400 scopus 로고    scopus 로고
    • Uniformly aligned full-length membrane proteins in liquid-crystalline bilayers for structural characterization
    • Li C., Gao F.P., Qin H., Chase R., Gor'kov P.L., Brey W.W., and Cross T.A. Uniformly aligned full-length membrane proteins in liquid-crystalline bilayers for structural characterization. J. Am. Chem. Soc. 129 (2007) 5304-5305
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 5304-5305
    • Li, C.1    Gao, F.P.2    Qin, H.3    Chase, R.4    Gor'kov, P.L.5    Brey, W.W.6    Cross, T.A.7
  • 57
    • 33846595904 scopus 로고
    • High resolution heteronuclear dipolar solid-state NMR spectroscopy
    • Wu C.H., Ramamoorthy A., and Opella S.J. High resolution heteronuclear dipolar solid-state NMR spectroscopy. J. Magn. Reson., Ser. A 109 (1994) 270-272
    • (1994) J. Magn. Reson., Ser. A , vol.109 , pp. 270-272
    • Wu, C.H.1    Ramamoorthy, A.2    Opella, S.J.3
  • 58
    • 0034186215 scopus 로고    scopus 로고
    • A solid-state NMR index of helical membrane proteins structure and topology
    • Marassi F.M., and Opella S.J. A solid-state NMR index of helical membrane proteins structure and topology. J. Magn. Reson. 144 (2000) 150-155
    • (2000) J. Magn. Reson. , vol.144 , pp. 150-155
    • Marassi, F.M.1    Opella, S.J.2
  • 60
    • 33846562986 scopus 로고    scopus 로고
    • Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies
    • Ramamoorthy A., Kandasamy S.K., Lee D.K., Kidambi S., and Larson R.G. Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies. Biochemistry 46 (2007) 965-975
    • (2007) Biochemistry , vol.46 , pp. 965-975
    • Ramamoorthy, A.1    Kandasamy, S.K.2    Lee, D.K.3    Kidambi, S.4    Larson, R.G.5
  • 61
    • 36849046108 scopus 로고    scopus 로고
    • R. Fu, M. Truong, R.J. Saager, M. Cotten, T.A. Cross, High resolution correlation spectroscopy in solid state NMR of aligned samples. J. Magn. Reson. (in press).
  • 62
    • 34748899645 scopus 로고    scopus 로고
    • Structural biology of transmembrane domains: efficient production and characterization of transmembrane peptides by NMR
    • Hu J., Qin H., Li C., Sharma M., Cross T.A., and Gao F.P. Structural biology of transmembrane domains: efficient production and characterization of transmembrane peptides by NMR. Protein Sci. 16 (2007) 2153-2165
    • (2007) Protein Sci. , vol.16 , pp. 2153-2165
    • Hu, J.1    Qin, H.2    Li, C.3    Sharma, M.4    Cross, T.A.5    Gao, F.P.6
  • 63
    • 33947171594 scopus 로고    scopus 로고
    • NMR of membrane proteins in micelles and bilayers: the FXYD family proteins
    • Franzin C.M., Gong X.-M., Thai K., Yu J., and Marassi F.M. NMR of membrane proteins in micelles and bilayers: the FXYD family proteins. Methods 41 (2007) 398-408
    • (2007) Methods , vol.41 , pp. 398-408
    • Franzin, C.M.1    Gong, X.-M.2    Thai, K.3    Yu, J.4    Marassi, F.M.5
  • 64
    • 34447135010 scopus 로고    scopus 로고
    • Structural similarity of a membrane protein in micelles and membranes
    • Franzin C.M., Teriete P., and Marassi F.M. Structural similarity of a membrane protein in micelles and membranes. J. Am. Chem. Soc. 129 (2007) 8078-8079
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 8078-8079
    • Franzin, C.M.1    Teriete, P.2    Marassi, F.M.3
  • 65
    • 33748479782 scopus 로고    scopus 로고
    • Structural dynamics and topology of phospholambin in oriented lipid bilayers using multidimensional solid state NMR
    • Traaseth N.J., Buffy J.J., Zamoon J., and Veglia G. Structural dynamics and topology of phospholambin in oriented lipid bilayers using multidimensional solid state NMR. Biochemistry 45 (2006) 13827-13834
    • (2006) Biochemistry , vol.45 , pp. 13827-13834
    • Traaseth, N.J.1    Buffy, J.J.2    Zamoon, J.3    Veglia, G.4
  • 68
    • 0030777711 scopus 로고    scopus 로고
    • Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation
    • Kovacs F., and Cross T.A. Transmembrane four-helix bundle of influenza A M2 protein channel: structural implications from helix tilt and orientation. Biophys. J. 73 (1997) 2511-2117
    • (1997) Biophys. J. , vol.73 , pp. 2511-2117
    • Kovacs, F.1    Cross, T.A.2
  • 69
    • 0034614541 scopus 로고    scopus 로고
    • Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property
    • Kovacs F.A., Denny J.K., Song Z., Quine J.R., and Cross T.A. Helix tilt of the M2 transmembrane peptide from influenza A virus: an intrinsic property. J. Mol. Biol. 295 (2000) 117-125
    • (2000) J. Mol. Biol. , vol.295 , pp. 117-125
    • Kovacs, F.A.1    Denny, J.K.2    Song, Z.3    Quine, J.R.4    Cross, T.A.5
  • 70
    • 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
  • 71
    • 0036787577 scopus 로고    scopus 로고
    • Uniformity, ideality and hydrogen bonds in transmembrane α-helices
    • Kim S., and Cross T.A. Uniformity, ideality and hydrogen bonds in transmembrane α-helices. Biophys. J. 83 (2002) 2084-2095
    • (2002) Biophys. J. , vol.83 , pp. 2084-2095
    • Kim, S.1    Cross, T.A.2
  • 72
    • 34447258592 scopus 로고    scopus 로고
    • The chemical and dynamical influence of the anti-viral drug amantadine on the M2 proton channel transmembrane domain
    • Hu J., Fu R., and Cross T.A. The chemical and dynamical influence of the anti-viral drug amantadine on the M2 proton channel transmembrane domain. Biophys. J. 93 (2007) 276-283
    • (2007) Biophys. J. , vol.93 , pp. 276-283
    • Hu, J.1    Fu, R.2    Cross, T.A.3
  • 74
    • 0023724614 scopus 로고
    • The solvent history dependence of gramicidin A conformations in hydrated lipid bilayers
    • LoGrasso P.V., Moll III F., and Cross T.A. The solvent history dependence of gramicidin A conformations in hydrated lipid bilayers. Biophys. J. 54 (1988) 259-267
    • (1988) Biophys. J. , vol.54 , pp. 259-267
    • LoGrasso, P.V.1    Moll III, F.2    Cross, T.A.3
  • 75
    • 0023733886 scopus 로고
    • The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes
    • Killian J.A., Prasad K.U., Hains D., and Urry D.W. The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes. Biochemistry 27 (1988) 4848-4855
    • (1988) Biochemistry , vol.27 , pp. 4848-4855
    • Killian, J.A.1    Prasad, K.U.2    Hains, D.3    Urry, D.W.4
  • 76
    • 0024295560 scopus 로고
    • New high performance liquid chromatography-based methodology for monitoring the conformational transitions of self-associating hydrophobic peptides, incorporated into liposomes
    • Bano M.C., Braco L., and Abad C. New high performance liquid chromatography-based methodology for monitoring the conformational transitions of self-associating hydrophobic peptides, incorporated into liposomes. J. Chromatogr. 458 (1988) 105-116
    • (1988) J. Chromatogr. , vol.458 , pp. 105-116
    • Bano, M.C.1    Braco, L.2    Abad, C.3
  • 77
    • 0024357363 scopus 로고
    • HPLC study on the 'history' dependence of gramicidin A conformation in phospholipid model membranes
    • Bano M.C., Braco L., and Abad C. HPLC study on the 'history' dependence of gramicidin A conformation in phospholipid model membranes. FEBS Lett. 250 (1989) 67-71
    • (1989) FEBS Lett. , vol.250 , pp. 67-71
    • Bano, M.C.1    Braco, L.2    Abad, C.3
  • 78
    • 0027142557 scopus 로고
    • Solvent history dependence of gramicidin-lipid interactions: a Raman and infrared spectroscopy study
    • Bouchard M., and Auger M. Solvent history dependence of gramicidin-lipid interactions: a Raman and infrared spectroscopy study. Biophys. J. 65 (1993) 2484-2492
    • (1993) Biophys. J. , vol.65 , pp. 2484-2492
    • Bouchard, M.1    Auger, M.2
  • 79
    • 0029038155 scopus 로고
    • Understanding the mechanism of action of the anti-influenza virus drug amantadine
    • Pinto L.H., and Lamb R.A. Understanding the mechanism of action of the anti-influenza virus drug amantadine. TRENDS Microbiol. 7 (1995) 271
    • (1995) TRENDS Microbiol. , vol.7 , pp. 271
    • Pinto, L.H.1    Lamb, R.A.2


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