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Volumn 6, Issue C, 1997, Pages 327-359

The dynamic nature of gramicidin

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EID: 77957064409     PISSN: 18745342     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-5342(96)80042-0     Document Type: Review
Times cited : (8)

References (151)
  • 1
    • 0028335099 scopus 로고
    • Conformation states of gramicidin A along the pathway to the formation of channels in model membranes determined by 2D NMR and circular dichroism
    • Abdul-Manan N., and Hinton J.F. Conformation states of gramicidin A along the pathway to the formation of channels in model membranes determined by 2D NMR and circular dichroism. Biochemistry 33 (1994) 6773-6783
    • (1994) Biochemistry , vol.33 , pp. 6773-6783
    • Abdul-Manan, N.1    Hinton, J.F.2
  • 2
    • 0025823857 scopus 로고
    • Proton conductance by the gramicidin water wire
    • Akeson M., and Deamer D.W. Proton conductance by the gramicidin water wire. Biophys. J. 60 (1991) 101-109
    • (1991) Biophys. J. , vol.60 , pp. 101-109
    • Akeson, M.1    Deamer, D.W.2
  • 3
  • 4
    • 0024331485 scopus 로고
    • Kinetics of ion movement mediated by carriers and channels
    • Andersen O.S. Kinetics of ion movement mediated by carriers and channels. Methods in Enzymol. 171 (1989) 62-112
    • (1989) Methods in Enzymol. , vol.171 , pp. 62-112
    • Andersen, O.S.1
  • 5
  • 8
    • 0000346708 scopus 로고
    • Gramicidin A transmembrane ion-channel. Three-dimensional structure reconstruction based on NMR-spectroscopy and energy refinement
    • Arseniev A.S., Lomize A.L., Barsukov I.L., and Bystrov V.F. Gramicidin A transmembrane ion-channel. Three-dimensional structure reconstruction based on NMR-spectroscopy and energy refinement. Biol. Membr. 3 (1986) 1077-1104
    • (1986) Biol. Membr. , vol.3 , pp. 1077-1104
    • Arseniev, A.S.1    Lomize, A.L.2    Barsukov, I.L.3    Bystrov, V.F.4
  • 9
    • 0017354373 scopus 로고
    • The action of a carbosuboxide dimerized gramicidin A on lipid bilayer membranes
    • Bamberg E., and Janko K. The action of a carbosuboxide dimerized gramicidin A on lipid bilayer membranes. Biochim. Biophys. Acta 465 (1977) 486-499
    • (1977) Biochim. Biophys. Acta , vol.465 , pp. 486-499
    • Bamberg, E.1    Janko, K.2
  • 10
    • 0017701531 scopus 로고
    • Blocking of the gramicidin channel by divalent cations
    • Bamberg E., and Lauger P. Blocking of the gramicidin channel by divalent cations. J. Membr. Biol. 35 (1977) 351-375
    • (1977) J. Membr. Biol. , vol.35 , pp. 351-375
    • Bamberg, E.1    Lauger, P.2
  • 11
    • 0025963698 scopus 로고
    • Conformation transitions of gramicidin A in phospholipid model membranes. A high performance liquid chromatography accessment
    • Bano M.C., Braco L., and Abad C. Conformation transitions of gramicidin A in phospholipid model membranes. A high performance liquid chromatography accessment. Biochemistry 30 (1991) 886-894
    • (1991) Biochemistry , vol.30 , pp. 886-894
    • Bano, M.C.1    Braco, L.2    Abad, C.3
  • 12
    • 0026716963 scopus 로고
    • A semi-empirical approach for the simulation of circular dichroism spectra of gramicidin A in a model membrane
    • Bano M.C., Braco L., and Abad C. A semi-empirical approach for the simulation of circular dichroism spectra of gramicidin A in a model membrane. Biophys. J. 63 (1992) 70-77
    • (1992) Biophys. J. , vol.63 , pp. 70-77
    • Bano, M.C.1    Braco, L.2    Abad, C.3
  • 14
    • 0025721931 scopus 로고
    • Amino acid sequence modulation of gramicidin channel function: Effects of tryptophan-to-phenylalanine substitutions on the single channel conductance and duration
    • Becker M.D., Greathouse D.V., Koeppe II R.E., and Andersen O.S. Amino acid sequence modulation of gramicidin channel function: Effects of tryptophan-to-phenylalanine substitutions on the single channel conductance and duration. Biochemistry 30 (1991) 8830-8839
    • (1991) Biochemistry , vol.30 , pp. 8830-8839
    • Becker, M.D.1    Greathouse, D.V.2    Koeppe II, R.E.3    Andersen, O.S.4
  • 15
    • 0027293465 scopus 로고
    • Influence of the nature of the aromatic side-chain on the conductance of the channel of linear gramicidin: Study of a series of 9, 11, 13, 15-Tyr (O-protected) derivatives
    • Benamer D., Daumas P., Trudelle Y., Calas B., Bennes R., and Heitz F. Influence of the nature of the aromatic side-chain on the conductance of the channel of linear gramicidin: Study of a series of 9, 11, 13, 15-Tyr (O-protected) derivatives. Eur. Biophys. J. 22 (1993) 145-150
    • (1993) Eur. Biophys. J. , vol.22 , pp. 145-150
    • Benamer, D.1    Daumas, P.2    Trudelle, Y.3    Calas, B.4    Bennes, R.5    Heitz, F.6
  • 16
    • 0027142557 scopus 로고
    • Solvent history dependence of gramicidin-lipid interactions: A Raman and infrared spectroscopic study
    • Bouchard M., and Auger M. Solvent history dependence of gramicidin-lipid interactions: A Raman and infrared spectroscopic study. Biophys. J. 65 (1993) 2484-2492
    • (1993) Biophys. J. , vol.65 , pp. 2484-2492
    • Bouchard, M.1    Auger, M.2
  • 17
    • 0343347931 scopus 로고
    • Monitoring self-association of a hydrophobic peptide with high performance liquid chromatography
    • Braco L., Bano M.C., and Abad C. Monitoring self-association of a hydrophobic peptide with high performance liquid chromatography. J. Chem. Edu. 69 (1992) A113-A116
    • (1992) J. Chem. Edu. , vol.69
    • Braco, L.1    Bano, M.C.2    Abad, C.3
  • 18
    • 0026724524 scopus 로고
    • Inhibition of gramicidin channel activity by local anaesthetics
    • Bridal T.R., and Busath D. Inhibition of gramicidin channel activity by local anaesthetics. Biochim. Biophys. Acta 1107 (1992) 31-38
    • (1992) Biochim. Biophys. Acta , vol.1107 , pp. 31-38
    • Bridal, T.R.1    Busath, D.2
  • 19
    • 0023084426 scopus 로고
    • On the conductance heterogeneity in membrane channels formed by gramicidin A. A cooperative study
    • Busath D., Andersen O.S., and Koeppe II R.E. On the conductance heterogeneity in membrane channels formed by gramicidin A. A cooperative study. Biophys. J. 51 (1987) 79-88
    • (1987) Biophys. J. , vol.51 , pp. 79-88
    • Busath, D.1    Andersen, O.S.2    Koeppe II, R.E.3
  • 21
    • 0023930650 scopus 로고
    • Permeation characteristics of gramicidin conformers
    • Busath D., and Szabo G. Permeation characteristics of gramicidin conformers. Biophys J. 53 (1988) 697-707
    • (1988) Biophys J. , vol.53 , pp. 697-707
    • Busath, D.1    Szabo, G.2
  • 22
    • 0027533833 scopus 로고
    • The use of physical methods in determining gramicidin channel structure and function
    • Busath D. The use of physical methods in determining gramicidin channel structure and function. Ann. Rev. Physiol. 55 (1993) 473-501
    • (1993) Ann. Rev. Physiol. , vol.55 , pp. 473-501
    • Busath, D.1
  • 23
    • 0027536384 scopus 로고
    • Biochemical characterization and crystallization of porin from Rhodopseudomonas blastica
    • Butz S., Benz R., Wacker T., Welte W., Lustig A., Plapp R., and Weckesser J. Biochemical characterization and crystallization of porin from Rhodopseudomonas blastica. Arch. Microbiol. 159 (1993) 301-307
    • (1993) Arch. Microbiol. , vol.159 , pp. 301-307
    • Butz, S.1    Benz, R.2    Wacker, T.3    Welte, W.4    Lustig, A.5    Plapp, R.6    Weckesser, J.7
  • 25
    • 0011262383 scopus 로고
    • The structure of the transmembrane channel of gramicidin A: NMR study of its conformation stability and interaction with divalent cations
    • Bystrov V.F., Arseniev A.S., Barsukov I.L., Golovanov A.P., and Maslennikov I.V. The structure of the transmembrane channel of gramicidin A: NMR study of its conformation stability and interaction with divalent cations. Gazz. Chim. Ital. 120 (1990) 485-491
    • (1990) Gazz. Chim. Ital. , vol.120 , pp. 485-491
    • Bystrov, V.F.1    Arseniev, A.S.2    Barsukov, I.L.3    Golovanov, A.P.4    Maslennikov, I.V.5
  • 26
    • 0027262294 scopus 로고
    • Total synthesis and ionophoric behaviour of gramicidin A analogue
    • Calmes M., Daunis J., David D., and Lazaro R. Total synthesis and ionophoric behaviour of gramicidin A analogue. Tetrahedron Letts. 34 (1993) 3275-3278
    • (1993) Tetrahedron Letts. , vol.34 , pp. 3275-3278
    • Calmes, M.1    Daunis, J.2    David, D.3    Lazaro, R.4
  • 27
    • 0025895720 scopus 로고
    • Time-correlation analysis of a simulated water motion in flexible and rigid gramicidin channels
    • Chiu S., Jakobsson E., Subramaniam S., and McCammon J.A. Time-correlation analysis of a simulated water motion in flexible and rigid gramicidin channels. Biophys. J. 60 (1991) 273-285
    • (1991) Biophys. J. , vol.60 , pp. 273-285
    • Chiu, S.1    Jakobsson, E.2    Subramaniam, S.3    McCammon, J.A.4
  • 28
    • 0024375490 scopus 로고
    • Water and polypeptide conformations in the gramicidin channel. A molecular dynamics study
    • Chiu S., Subramaniam S., Jakobsson E., and McCammon J.A. Water and polypeptide conformations in the gramicidin channel. A molecular dynamics study. Biophys. J. 56 (1989) 253-261
    • (1989) Biophys. J. , vol.56 , pp. 253-261
    • Chiu, S.1    Subramaniam, S.2    Jakobsson, E.3    McCammon, J.A.4
  • 29
    • 0026576290 scopus 로고
    • Supramolecular organization of gramicidin channels. The elementary conducting unit is a dimer
    • Cifu A.S., Koeppe II R.E., and Andersen O.S. Supramolecular organization of gramicidin channels. The elementary conducting unit is a dimer. Biophys. J. 61 (1992) 189-203
    • (1992) Biophys. J. , vol.61 , pp. 189-203
    • Cifu, A.S.1    Koeppe II, R.E.2    Andersen, O.S.3
  • 32
    • 0026524801 scopus 로고
    • Gramicidin conformational studies with mixed-chain unsaturated phospholipid bilayer systems
    • Cox K.J., Ho C., Lombardi J.V., and Stubbs O.D. Gramicidin conformational studies with mixed-chain unsaturated phospholipid bilayer systems. Biochem. 31 (1992) 1112-1118
    • (1992) Biochem. , vol.31 , pp. 1112-1118
    • Cox, K.J.1    Ho, C.2    Lombardi, J.V.3    Stubbs, O.D.4
  • 33
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional role of lipids in biological membranes
    • Cullis P.R., and De Kruijff B. Lipid polymorphism and the functional role of lipids in biological membranes. Biochim. Biophys. Acta 559 (1979) 399-420
    • (1979) Biochim. Biophys. Acta , vol.559 , pp. 399-420
    • Cullis, P.R.1    De Kruijff, B.2
  • 36
    • 0025356022 scopus 로고
    • A quantitative infrared determination of acyl chain conformation in gramicidin/dipalmitoylphosphatidylcholine bilayers
    • Davies M.A., Brauner J.W., Schuster H.F., and Mendelsohn R. A quantitative infrared determination of acyl chain conformation in gramicidin/dipalmitoylphosphatidylcholine bilayers. Biochem. Biophys. Res. Comm. 168 (1990) 85-90
    • (1990) Biochem. Biophys. Res. Comm. , vol.168 , pp. 85-90
    • Davies, M.A.1    Brauner, J.W.2    Schuster, H.F.3    Mendelsohn, R.4
  • 37
    • 77957074234 scopus 로고
    • Role of water in proton flux mechanisms
    • Gaber B.P., and Easwaran K.D.K. (Eds), Adenine Press, Guilderland, N.Y.
    • Deamer D.W. Role of water in proton flux mechanisms. In: Gaber B.P., and Easwaran K.D.K. (Eds). Biomembranes Structure and Function-The State of the Art (1992), Adenine Press, Guilderland, N.Y. 209-225
    • (1992) Biomembranes Structure and Function-The State of the Art , pp. 209-225
    • Deamer, D.W.1
  • 38
    • 0024503168 scopus 로고
    • Proton flux mechanisms in model and biological membranes
    • Deamer D.W., and Nichols J.W. Proton flux mechanisms in model and biological membranes. J. Membr. Biol. 107 (1989) 91-103
    • (1989) J. Membr. Biol. , vol.107 , pp. 91-103
    • Deamer, D.W.1    Nichols, J.W.2
  • 39
    • 0023701797 scopus 로고
    • + ion conductance through the gramicidin channel
    • + ion conductance through the gramicidin channel. Biophys. J. 53 (1988) 25-32
    • (1988) Biophys. J. , vol.53 , pp. 25-32
    • Decker, E.R.1    Levitt, D.G.2
  • 40
    • 0021755973 scopus 로고
    • X-ray structure analysis of a membrane protein complex: Electron density map at 3 resolution and a model of the chromophores of the photosynthetic reaction centre from Rhodopseudomonas viridis
    • Deisenhofer J., Epp O., Miki K., Huber R., and Michel H. X-ray structure analysis of a membrane protein complex: Electron density map at 3 resolution and a model of the chromophores of the photosynthetic reaction centre from Rhodopseudomonas viridis. J. Mol. Biol. 180 (1984) 385-398
    • (1984) J. Mol. Biol. , vol.180 , pp. 385-398
    • Deisenhofer, J.1    Epp, O.2    Miki, K.3    Huber, R.4    Michel, H.5
  • 41
    • 0037644416 scopus 로고
    • The structure of the gramicidin/KSCN complex
    • Doyle D.A., and Wallace B.A. The structure of the gramicidin/KSCN complex. Biophys. J. 66 (1994) 353
    • (1994) Biophys. J. , vol.66 , pp. 353
    • Doyle, D.A.1    Wallace, B.A.2
  • 42
    • 0028096948 scopus 로고
    • Caesium-binding sites in the gramicidin pore
    • Doyle D.A., and Wallace B.A. Caesium-binding sites in the gramicidin pore. Biochem. Soc. Trans. 22 (1994) 1043-1045
    • (1994) Biochem. Soc. Trans. , vol.22 , pp. 1043-1045
    • Doyle, D.A.1    Wallace, B.A.2
  • 44
    • 0018826901 scopus 로고
    • The permeability of the endplate channel to organic cations in frog muscle
    • Dwyer T.M., Adams D.J., and Hille B. The permeability of the endplate channel to organic cations in frog muscle. J. Gen. Physiol. 75 (1980) 469-492
    • (1980) J. Gen. Physiol. , vol.75 , pp. 469-492
    • Dwyer, T.M.1    Adams, D.J.2    Hille, B.3
  • 45
    • 0019795013 scopus 로고
    • The gramicidin A channel: A review of its permeability characteristics with special reference to the single-file aspect of transport
    • Finkelstein A., and Andersen O.S. The gramicidin A channel: A review of its permeability characteristics with special reference to the single-file aspect of transport. J. Membr. Biol. 59 (1981) 155-171
    • (1981) J. Membr. Biol. , vol.59 , pp. 155-171
    • Finkelstein, A.1    Andersen, O.S.2
  • 47
    • 0020000210 scopus 로고
    • Blocking kinetics of the anomalous potassium rectifier of tunicate egg studied by single channel recording
    • Fukushima Y. Blocking kinetics of the anomalous potassium rectifier of tunicate egg studied by single channel recording. J. Physiol. 331 (1982) 311-331
    • (1982) J. Physiol. , vol.331 , pp. 311-331
    • Fukushima, Y.1
  • 48
    • 0023241763 scopus 로고
    • Effect of calcium on the gramicidin A single channel in phosphatidylserine membranes
    • Gambale F., Menini A., and Rauch G. Effect of calcium on the gramicidin A single channel in phosphatidylserine membranes. Eur. Biophys. J. 14 (1987) 369-374
    • (1987) Eur. Biophys. J. , vol.14 , pp. 369-374
    • Gambale, F.1    Menini, A.2    Rauch, G.3
  • 49
    • 0027488790 scopus 로고
    • An electron spin resonance study of interactions between gramicidin A and phosphatidylcholine bilayers
    • Ge M., and Freed J.H. An electron spin resonance study of interactions between gramicidin A and phosphatidylcholine bilayers. Biophys. J. 65 (1993) 2106-2123
    • (1993) Biophys. J. , vol.65 , pp. 2106-2123
    • Ge, M.1    Freed, J.H.2
  • 51
    • 0001168290 scopus 로고
    • Gramicidin. IX. Preparation of gramicidin A, B, and C
    • Gross E., and Witkop B. Gramicidin. IX. Preparation of gramicidin A, B, and C. Biochemistry 4 (1965) 2495-2501
    • (1965) Biochemistry , vol.4 , pp. 2495-2501
    • Gross, E.1    Witkop, B.2
  • 53
    • 0027459169 scopus 로고
    • X-ray scattering with momentum transfer in the plane of membrane. Application to gramicidin organization
    • He K., Ludtke S.J., Wu Y., and Huang H.W. X-ray scattering with momentum transfer in the plane of membrane. Application to gramicidin organization. Biophys. J. 64 (1993) 157-162
    • (1993) Biophys. J. , vol.64 , pp. 157-162
    • He, K.1    Ludtke, S.J.2    Wu, Y.3    Huang, H.W.4
  • 55
    • 0023687105 scopus 로고
    • Open channel noise. IV. Estimates of rapid kinetics of formamide block in gramicidin A channel
    • Heinmann S.H., and Sigworth F.J. Open channel noise. IV. Estimates of rapid kinetics of formamide block in gramicidin A channel. Biophys. J. 54 (1988) 757-764
    • (1988) Biophys. J. , vol.54 , pp. 757-764
    • Heinmann, S.H.1    Sigworth, F.J.2
  • 56
    • 0025342169 scopus 로고
    • Open channel noise. V. Fluctuating barriers to ion entry in gramicidin A channels
    • Heinmann S.H., and Sigworth F.J. Open channel noise. V. Fluctuating barriers to ion entry in gramicidin A channels. Biophys. J. 57 (1990) 499-514
    • (1990) Biophys. J. , vol.57 , pp. 499-514
    • Heinmann, S.H.1    Sigworth, F.J.2
  • 57
    • 77957078853 scopus 로고
    • Conformations of gramicidin A and its 9, 11, 13, 15-phenylalanyl analog in dimethylsulfoxide and chloroform
    • Heitz F., Heitz A., and Trudelle Y. Conformations of gramicidin A and its 9, 11, 13, 15-phenylalanyl analog in dimethylsulfoxide and chloroform. Biophys. Chem. 166 (1986) 437-445
    • (1986) Biophys. Chem. , vol.166 , pp. 437-445
    • Heitz, F.1    Heitz, A.2    Trudelle, Y.3
  • 58
    • 0025231220 scopus 로고
    • Calculations of deformation energies and conformations in lipid membrane containing gramicidin channels
    • Helfrich P., and Jakobsson E. Calculations of deformation energies and conformations in lipid membrane containing gramicidin channels. Biophys. J. 57 (1990) 1075-1084
    • (1990) Biophys. J. , vol.57 , pp. 1075-1084
    • Helfrich, P.1    Jakobsson, E.2
  • 59
    • 0025847306 scopus 로고
    • Small iminium ions block gramicidin channels in lipid bilayers
    • Hemsley G., and Busath D. Small iminium ions block gramicidin channels in lipid bilayers. Biophys. J. 59 (1991) 901-908
    • (1991) Biophys. J. , vol.59 , pp. 901-908
    • Hemsley, G.1    Busath, D.2
  • 62
    • 0027219740 scopus 로고
    • 3-gA in multilamellar dimyristoylphosphatidylcholine dispersions
    • 3-gA in multilamellar dimyristoylphosphatidylcholine dispersions. Biochemistry 32 (1993) 7593-7604
    • (1993) Biochemistry , vol.32 , pp. 7593-7604
    • Hing, A.W.1    Schaefer, J.2
  • 63
    • 0027916206 scopus 로고
    • 23Na-NMR study of ion transport across vesicle membranes facilitated by phenylalanine analogs of gramicidin
    • 23Na-NMR study of ion transport across vesicle membranes facilitated by phenylalanine analogs of gramicidin. Biochim. Biophys. Acta 1146 (1993) 191-196
    • (1993) Biochim. Biophys. Acta , vol.1146 , pp. 191-196
    • Hinton, J.F.1    Easton, P.L.2    Newkirk, D.A.3    Shungu, D.C.4
  • 65
    • 0015499206 scopus 로고
    • Ion transfer across lipid membranes in the presence of gramicidin A. I. Studies of the unit conductance channel
    • Hladky S.B., and Haydon D.A. Ion transfer across lipid membranes in the presence of gramicidin A. I. Studies of the unit conductance channel. Biochim. Biophys. Acta 274 (1972) 294-312
    • (1972) Biochim. Biophys. Acta , vol.274 , pp. 294-312
    • Hladky, S.B.1    Haydon, D.A.2
  • 66
    • 0026705715 scopus 로고
    • Hydration at the membrane protein-lipid interface
    • Ho C., and Stubbes C.D. Hydration at the membrane protein-lipid interface. Biophys. J. 63 (1992) 897-902
    • (1992) Biophys. J. , vol.63 , pp. 897-902
    • Ho, C.1    Stubbes, C.D.2
  • 67
    • 0027198547 scopus 로고
    • Tryptophans in membrane proteins: Indole ring orientations and functional implications in the gramicidin channel
    • Hu W., Lee K.C., and Cross T.A. Tryptophans in membrane proteins: Indole ring orientations and functional implications in the gramicidin channel. Biochemistry 32 (1993) 7035-7047
    • (1993) Biochemistry , vol.32 , pp. 7035-7047
    • Hu, W.1    Lee, K.C.2    Cross, T.A.3
  • 68
    • 33845282559 scopus 로고
    • Microscopic approaches to ion transport through transmembrane channels. The model system gramicidin
    • Jordan P.C. Microscopic approaches to ion transport through transmembrane channels. The model system gramicidin. J. Phys. Chem. 91 (1987) 6582-6591
    • (1987) J. Phys. Chem. , vol.91 , pp. 6582-6591
    • Jordan, P.C.1
  • 69
    • 0026594687 scopus 로고
    • Constant helical pitch of the gramicidin channel in phospholipid bilayers
    • Katsaras J., Prosser R.S., Stinson R.H., and Davis J.H. Constant helical pitch of the gramicidin channel in phospholipid bilayers. Biophys. J. 61 (1992) 827-830
    • (1992) Biophys. J. , vol.61 , pp. 827-830
    • Katsaras, J.1    Prosser, R.S.2    Stinson, R.H.3    Davis, J.H.4
  • 70
    • 0027360175 scopus 로고
    • High resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • Ketchem R.R., Hu W., and Cross T.A. High resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science 261 (1993) 1457-1460
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 71
    • 0026473040 scopus 로고
    • Gramicidin and gramicidin-lipid interactions
    • Killian J.A. Gramicidin and gramicidin-lipid interactions. Biochim. Biophys. Acta 1113 (1992) 391-425
    • (1992) Biochim. Biophys. Acta , vol.1113 , pp. 391-425
    • Killian, J.A.1
  • 72
    • 0023704908 scopus 로고
    • II phase induction by gramicidin in model membranes and its relation to channel function
    • II phase induction by gramicidin in model membranes and its relation to channel function. Biophys. J. 53 (1988) 111-117
    • (1988) Biophys. J. , vol.53 , pp. 111-117
    • Killian, J.A.1    De Kruijff, B.2
  • 74
    • 0023733886 scopus 로고
    • The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behaviour 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 behaviour 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
  • 75
    • 0000708966 scopus 로고
    • Crystalline ion complexes of gramicidin A
    • Kimball M.R., and Wallace B.A. Crystalline ion complexes of gramicidin A. Annals N.Y. Acad. Sci. 435 (1984) 551-554
    • (1984) Annals N.Y. Acad. Sci. , vol.435 , pp. 551-554
    • Kimball, M.R.1    Wallace, B.A.2
  • 76
    • 0017820506 scopus 로고
    • Helical channels in crystals of a cesium-gramicidin A complex: An X-ray diffraction study
    • Koeppe II R.E., Hodgson K.O., and Stryer L. Helical channels in crystals of a cesium-gramicidin A complex: An X-ray diffraction study. J. Mol. Biol. 1221 (1978) 41-54
    • (1978) J. Mol. Biol. , vol.1221 , pp. 41-54
    • Koeppe II, R.E.1    Hodgson, K.O.2    Stryer, L.3
  • 77
    • 0021854185 scopus 로고
    • Gramicidin-K, a new linear channel-forming gramicidin from Bacillus brevis
    • Koeppe II R.E., Paczkowski J.A., and Whaley W.L. Gramicidin-K, a new linear channel-forming gramicidin from Bacillus brevis. Biochem. 12 (1985) 2822-2826
    • (1985) Biochem. , vol.12 , pp. 2822-2826
    • Koeppe II, R.E.1    Paczkowski, J.A.2    Whaley, W.L.3
  • 79
    • 0025017338 scopus 로고
    • Distinction between dipolar and inductive effects in modulating the conductance of gramicidin
    • Koeppe II R.E., Mazet J., and Andersen O.S. Distinction between dipolar and inductive effects in modulating the conductance of gramicidin. Biochem. 29 (1990) 512-520
    • (1990) Biochem. , vol.29 , pp. 512-520
    • Koeppe II, R.E.1    Mazet, J.2    Andersen, O.S.3
  • 80
    • 0028045061 scopus 로고
    • Orientation of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy
    • Koeppe II R.E., Killian J.A., and Greathouse D.V. Orientation of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy. Biophys. J. 66 (1994) 14-24
    • (1994) Biophys. J. , vol.66 , pp. 14-24
    • Koeppe II, R.E.1    Killian, J.A.2    Greathouse, D.V.3
  • 81
    • 0027499143 scopus 로고
    • Non-random distribution of the amino-acids in the transmembrane segments of the human type I single span membrane proteins
    • Landolt-Marticorena C., Williams K.A., Deber C.M., and Reithmeier R.A.F. Non-random distribution of the amino-acids in the transmembrane segments of the human type I single span membrane proteins. J. Mol. Biol. 229 (1993) 602-608
    • (1993) J. Mol. Biol. , vol.229 , pp. 602-608
    • Landolt-Marticorena, C.1    Williams, K.A.2    Deber, C.M.3    Reithmeier, R.A.F.4
  • 82
    • 0024281641 scopus 로고
    • Three dimensional structure at 0.86 of the uncomplexed form of the transmembrane ion channel peptide gramicidin A
    • Langs D.A. Three dimensional structure at 0.86 of the uncomplexed form of the transmembrane ion channel peptide gramicidin A. Science 241 (1988) 188-191
    • (1988) Science , vol.241 , pp. 188-191
    • Langs, D.A.1
  • 83
    • 33646791189 scopus 로고
    • Ab initio direct methods: Practical advice for getting beyond the first 300 atoms
    • Langs D.A. Ab initio direct methods: Practical advice for getting beyond the first 300 atoms. Acta Cryst. D49 (1993) 158-167
    • (1993) Acta Cryst. , vol.D49 , pp. 158-167
    • Langs, D.A.1
  • 85
    • 0022470774 scopus 로고
    • 2+. Voltage and concentration dependence of calcium entry into the pore
    • 2+. Voltage and concentration dependence of calcium entry into the pore. J. Gen. Physiol. 88 (1986) 321-347
    • (1986) J. Gen. Physiol. , vol.88 , pp. 321-347
    • Lansman, J.B.1    Hess, P.2    Tsien, R.W.3
  • 86
    • 0023518403 scopus 로고
    • Dynamics of ion transport systems in membranes
    • Lauger P. Dynamics of ion transport systems in membranes. Physiol. Rev. 67 (1987) 1296-1331
    • (1987) Physiol. Rev. , vol.67 , pp. 1296-1331
    • Lauger, P.1
  • 87
    • 0344381025 scopus 로고
    • Sterol-dependent inactivation of gramicidin-A induced ionic channels in the cell and artificial lipid-bilayer membrane
    • Lev A.A. Sterol-dependent inactivation of gramicidin-A induced ionic channels in the cell and artificial lipid-bilayer membrane. Biophys. Membr. Transp. 1 (1990) 231-250
    • (1990) Biophys. Membr. Transp. , vol.1 , pp. 231-250
    • Lev, A.A.1
  • 88
    • 0023724614 scopus 로고
    • Solvent history dependence of gramicidin A conformations in hydrated lipid bilayers
    • LoGrasso P.V., Moll III F., and Cross T.A. 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
  • 89
    • 0027424975 scopus 로고
    • Electrostatic interactions in gramicidin channels. Three-dielectric model
    • Martinez G., and Sancho M. Electrostatic interactions in gramicidin channels. Three-dielectric model. Eur. Biophys. J. 22 (1993) 301-307
    • (1993) Eur. Biophys. J. , vol.22 , pp. 301-307
    • Martinez, G.1    Sancho, M.2
  • 90
    • 0019163618 scopus 로고
    • Conformational studies on the gramicidin A transmembrane channel in lipid micelles and liposomes
    • Masotti L., Spisni A., and Urry D.W. Conformational studies on the gramicidin A transmembrane channel in lipid micelles and liposomes. Cell Biophys. 2 (1980) 241-251
    • (1980) Cell Biophys. , vol.2 , pp. 241-251
    • Masotti, L.1    Spisni, A.2    Urry, D.W.3
  • 91
    • 0021322832 scopus 로고
    • Single-channel studies on linear gramicidins with altered amino-acid sequences-a comparison of phenylalanine, tryptophane, and tyrosine substitutions at position-1 and position-11
    • Mazet J.L., Andersen O.S., and Koeppe II R.E. Single-channel studies on linear gramicidins with altered amino-acid sequences-a comparison of phenylalanine, tryptophane, and tyrosine substitutions at position-1 and position-11. Biophys. J. 45 (1984) 263-276
    • (1984) Biophys. J. , vol.45 , pp. 263-276
    • Mazet, J.L.1    Andersen, O.S.2    Koeppe II, R.E.3
  • 93
    • 0020475570 scopus 로고
    • Three-dimensional crystals of a membrane protein complex
    • Michel H. Three-dimensional crystals of a membrane protein complex. J. Mol. Biol. 158 (1982) 567-572
    • (1982) J. Mol. Biol. , vol.158 , pp. 567-572
    • Michel, H.1
  • 94
    • 0027332363 scopus 로고
    • 2+-induced lateral phase separation in black lipid membranes and its coupling to the ion-translocation by gramicidin
    • 2+-induced lateral phase separation in black lipid membranes and its coupling to the ion-translocation by gramicidin. Biochim. Biophys. Acta 1152 (1993) 259-269
    • (1993) Biochim. Biophys. Acta , vol.1152 , pp. 259-269
    • Mittler-Neher, S.1    Knoll, W.2
  • 95
    • 0018801170 scopus 로고
    • Transmembrane channel activity of gramicidin A analogs: Effects of modification and deletion of the amino-terminal residue
    • Morrow J.S., Veatch W.R., and Stryler L. Transmembrane channel activity of gramicidin A analogs: Effects of modification and deletion of the amino-terminal residue. J. Mol. Biol. 132 (1979) 733-738
    • (1979) J. Mol. Biol. , vol.132 , pp. 733-738
    • Morrow, J.S.1    Veatch, W.R.2    Stryler, L.3
  • 96
    • 0028352135 scopus 로고
    • Motionally restricted tryptophan environments at the peptide-lipid interface of gramicidin channels
    • Mukherjee S., and Chattopadhyay A. Motionally restricted tryptophan environments at the peptide-lipid interface of gramicidin channels. Biochemistry 33 (1994) 5089-5097
    • (1994) Biochemistry , vol.33 , pp. 5089-5097
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 97
    • 0015499163 scopus 로고
    • Ion transfer across lipid membranes in the presence of gramicidin A. II. The ion selectivity
    • Myers V.B., and Haydon D.A. Ion transfer across lipid membranes in the presence of gramicidin A. II. The ion selectivity. Biochim. Biophys. Acta 274 (1972) 313-322
    • (1972) Biochim. Biophys. Acta , vol.274 , pp. 313-322
    • Myers, V.B.1    Haydon, D.A.2
  • 98
    • 0019976513 scopus 로고
    • Orientation of gramicidin A transmembrane channel
    • Nabedryk E., Gingold M.P., and Breton J. Orientation of gramicidin A transmembrane channel. Biophys. J. 38 (1982) 243-249
    • (1982) Biophys. J. , vol.38 , pp. 243-249
    • Nabedryk, E.1    Gingold, M.P.2    Breton, J.3
  • 99
    • 0016818713 scopus 로고
    • Ionic selectivity of the gramicidin channel and the thallous ion
    • Neher E. Ionic selectivity of the gramicidin channel and the thallous ion. Biophys. J. 401 (1975) 540-544
    • (1975) Biophys. J. , vol.401 , pp. 540-544
    • Neher, E.1
  • 100
    • 37049081301 scopus 로고
    • Effect of lipid charge and solution composition on the permeability of phospholipid-gramicidin monolayers to Tl
    • Nelson A. Effect of lipid charge and solution composition on the permeability of phospholipid-gramicidin monolayers to Tl. J. Chem. Soc. Far. Trans. 89 (1993) 2799-2805
    • (1993) J. Chem. Soc. Far. Trans. , vol.89 , pp. 2799-2805
    • Nelson, A.1
  • 101
    • 0026683664 scopus 로고
    • A dipolar amino acid substitution induces voltage-dependent transitions between two stable conductance states in gramicidin channels
    • Oiki S., Koeppe II R.E., and Andersen O.S. A dipolar amino acid substitution induces voltage-dependent transitions between two stable conductance states in gramicidin channels. Biophys. J. 62 (1992) 28-30
    • (1992) Biophys. J. , vol.62 , pp. 28-30
    • Oiki, S.1    Koeppe II, R.E.2    Andersen, O.S.3
  • 102
    • 0025878348 scopus 로고
    • Location of ion binding sites in the gramicidin channel by X-ray diffraction
    • Olah G.A., Huang H.W., and Wu Y. Location of ion binding sites in the gramicidin channel by X-ray diffraction. J. Mol. Biol. 218 (1991) 847-858
    • (1991) J. Mol. Biol. , vol.218 , pp. 847-858
    • Olah, G.A.1    Huang, H.W.2    Wu, Y.3
  • 103
    • 0025923145 scopus 로고
    • 2H nuclear magnetic resonance of the gramicidin A backbone in a phospholipid bilayer
    • 2H nuclear magnetic resonance of the gramicidin A backbone in a phospholipid bilayer. Biochemistry 30 (1991) 4687-4696
    • (1991) Biochemistry , vol.30 , pp. 4687-4696
    • Prosser, R.S.1    Davis, J.H.2
  • 104
    • 0023445780 scopus 로고
    • Energy profiles in the gramicidin A channel
    • Pullman A. Energy profiles in the gramicidin A channel. Quart. Rev. Biophys. 20 (1987) 173-200
    • (1987) Quart. Rev. Biophys. , vol.20 , pp. 173-200
    • Pullman, A.1
  • 105
    • 0000397670 scopus 로고
    • Contribution of theoretical chemistry to the study of ion transport through membranes
    • Pullman A. Contribution of theoretical chemistry to the study of ion transport through membranes. Chem. Rev. 91 (1991) 793-812
    • (1991) Chem. Rev. , vol.91 , pp. 793-812
    • Pullman, A.1
  • 106
    • 0015307470 scopus 로고
    • Conformation of peptide chains containing both L- and D-residues: Part I-helical structures with alternating L- and D-residues with special reference to the LD-ribbon and the LD-helix
    • Ramachandran G.N., and Chandrasekaran R. Conformation of peptide chains containing both L- and D-residues: Part I-helical structures with alternating L- and D-residues with special reference to the LD-ribbon and the LD-helix. Ind. J. Biochem. 9 (1972) 1-11
    • (1972) Ind. J. Biochem. , vol.9 , pp. 1-11
    • Ramachandran, G.N.1    Chandrasekaran, R.2
  • 107
    • 0026633889 scopus 로고
    • Influence of ion occupancy and membrane deformation on gramicidin A channel stability in lipid membranes
    • Ring A. Influence of ion occupancy and membrane deformation on gramicidin A channel stability in lipid membranes. Biophys. J. 61 (1992) 1305-1315
    • (1992) Biophys. J. , vol.61 , pp. 1305-1315
    • Ring, A.1
  • 108
    • 0025882246 scopus 로고
    • Ion transport in a model gramicidin channel
    • Roux B., and Karplus M. Ion transport in a model gramicidin channel. Biophys. J. 59 (1991) 961-981
    • (1991) Biophys. J. , vol.59 , pp. 961-981
    • Roux, B.1    Karplus, M.2
  • 109
    • 33748583013 scopus 로고
    • Ion transport in a gramicidin like channel: Dynamics and mobility
    • Roux B., and Karplus M. Ion transport in a gramicidin like channel: Dynamics and mobility. J. Phys. Chem. 95 (1991) 4856-4868
    • (1991) J. Phys. Chem. , vol.95 , pp. 4856-4868
    • Roux, B.1    Karplus, M.2
  • 110
    • 0027232024 scopus 로고
    • Ion transport in the gramicidin channel: Free energy of the solvated right-handed dimer in a model membrane
    • Roux B., and Karplus M. Ion transport in the gramicidin channel: Free energy of the solvated right-handed dimer in a model membrane. J. Am. Chem. Soc. 115 (1993) 3250-3262
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3250-3262
    • Roux, B.1    Karplus, M.2
  • 111
    • 0028321565 scopus 로고
    • Molecular dynamic simulations of the gramicidin channel
    • Roux B., and Karplus M. Molecular dynamic simulations of the gramicidin channel. Ann. Rev. Biophys. Biomol. Struct. 23 (1994) 731-761
    • (1994) Ann. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 731-761
    • Roux, B.1    Karplus, M.2
  • 112
    • 33947482744 scopus 로고
    • Gramicidin A. V. The structure of valine- and isoleucine-gramicidin A
    • Sarges R., and Witkop B. Gramicidin A. V. The structure of valine- and isoleucine-gramicidin A. J. Am. Chem. Soc. 87 (1965) 2011-2020
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2011-2020
    • Sarges, R.1    Witkop, B.2
  • 113
    • 0025094633 scopus 로고
    • Gramicidin-A, gramicidin-B, and gramicidin-C form structurally equivalent ion channels
    • Sawyer D.B., Williams L.P., Whaley W.L., Koeppe II R.E., and Andersen O.S. Gramicidin-A, gramicidin-B, and gramicidin-C form structurally equivalent ion channels. Biophys. J. 58 (1990) 1207-1212
    • (1990) Biophys. J. , vol.58 , pp. 1207-1212
    • Sawyer, D.B.1    Williams, L.P.2    Whaley, W.L.3    Koeppe II, R.E.4    Andersen, O.S.5
  • 114
    • 0026051563 scopus 로고
    • Effect of increased chain packing on the gramicidin-lipid interactions
    • Scarlata S.F. Effect of increased chain packing on the gramicidin-lipid interactions. Biochemistry 30 (1991) 9853-9859
    • (1991) Biochemistry , vol.30 , pp. 9853-9859
    • Scarlata, S.F.1
  • 115
    • 77957087939 scopus 로고
    • The covalent modification of eukaryotic proteins with lipids
    • Sefton B.M., and Buss J.E. The covalent modification of eukaryotic proteins with lipids. J. Cell Biol. 155 (1987) 167-183
    • (1987) J. Cell Biol. , vol.155 , pp. 167-183
    • Sefton, B.M.1    Buss, J.E.2
  • 116
    • 0027200325 scopus 로고
    • The permeation properties of small organic cations in gramicidin A channels
    • Seoh S., and Busath D. The permeation properties of small organic cations in gramicidin A channels. Biophys. J. 64 (1993) 1017-1028
    • (1993) Biophys. J. , vol.64 , pp. 1017-1028
    • Seoh, S.1    Busath, D.2
  • 117
    • 0027420654 scopus 로고
    • Formamidinium-induced dimer stabilization and flicker block behaviour in homo- and heterodimer channels formed by gramicidin A and N-acetyl gramicidin A
    • Seoh S., and Busath D. Formamidinium-induced dimer stabilization and flicker block behaviour in homo- and heterodimer channels formed by gramicidin A and N-acetyl gramicidin A. Biophys. J. 65 (1993) 1817-1827
    • (1993) Biophys. J. , vol.65 , pp. 1817-1827
    • Seoh, S.1    Busath, D.2
  • 118
    • 0000481074 scopus 로고
    • NMR order parameter analysis of a peptide plane aligned in a lyotropic liquid crystal
    • Separovic F., Pax R., and Cornell B. NMR order parameter analysis of a peptide plane aligned in a lyotropic liquid crystal. Mol. Phys. 78 (1993) 357-369
    • (1993) Mol. Phys. , vol.78 , pp. 357-369
    • Separovic, F.1    Pax, R.2    Cornell, B.3
  • 119
    • 0022996029 scopus 로고
    • Investigation of the interaction between thallous ions and gramicidin A in dimyristoylphosphatidylcholine vesicles: A thallium-205 NMR equilibrium study
    • Shungu D.C., Hinton J.F., Koeppe II R.E., and Millett F.S. Investigation of the interaction between thallous ions and gramicidin A in dimyristoylphosphatidylcholine vesicles: A thallium-205 NMR equilibrium study. Biochemistry 25 (1986) 6103-6108
    • (1986) Biochemistry , vol.25 , pp. 6103-6108
    • Shungu, D.C.1    Hinton, J.F.2    Koeppe II, R.E.3    Millett, F.S.4
  • 120
    • 0021797982 scopus 로고
    • Open channel noise. I. Noise in acetylcholine receptor currents suggests conformational fluctuations
    • Sigworth F.J. Open channel noise. I. Noise in acetylcholine receptor currents suggests conformational fluctuations. Biophys. J. 47 (1985) 709-720
    • (1985) Biophys. J. , vol.47 , pp. 709-720
    • Sigworth, F.J.1
  • 125
    • 0023320530 scopus 로고
    • Why is gramicidin valence selective?
    • Sung S., and Jordan P.C. Why is gramicidin valence selective?. Biophys. J. 51 (1987) 661-672
    • (1987) Biophys. J. , vol.51 , pp. 661-672
    • Sung, S.1    Jordan, P.C.2
  • 126
    • 0027519324 scopus 로고
    • The double ππ5.6 helix of gramicidin A predominates in unsaturated lipid membranes
    • Sychev S.V., Barsukov L., and Ivanov V.Y. The double ππ5.6 helix of gramicidin A predominates in unsaturated lipid membranes. Eur. J. Biochem. 22 (1993) 279-288
    • (1993) Eur. J. Biochem. , vol.22 , pp. 279-288
    • Sychev, S.V.1    Barsukov, L.2    Ivanov, V.Y.3
  • 127
    • 0025103378 scopus 로고
    • Environments and conformations of tryptophan side chains of gramicidin A in phospholipid bilayers studied by Raman spectroscopy
    • Takeuchi H., Nemoto Y., and Harada I. Environments and conformations of tryptophan side chains of gramicidin A in phospholipid bilayers studied by Raman spectroscopy. Biochemistry 29 (1990) 1572-1579
    • (1990) Biochemistry , vol.29 , pp. 1572-1579
    • Takeuchi, H.1    Nemoto, Y.2    Harada, I.3
  • 128
    • 0025868281 scopus 로고
    • Effect of salt and membrane fluidity on fluorophore motions of a gramicidin C derivative
    • Teng Q., Koeppe II R.E., and Scarlata S.F. Effect of salt and membrane fluidity on fluorophore motions of a gramicidin C derivative. Biochemistry 30 (1991) 7984-7990
    • (1991) Biochemistry , vol.30 , pp. 7984-7990
    • Teng, Q.1    Koeppe II, R.E.2    Scarlata, S.F.3
  • 129
    • 0023664472 scopus 로고
    • Experimental and theoretical study of gramicidin P, an analog of gramicidin A with a methylamine C-terminal
    • Trudelle Y., Daumas P., Heitz F., Etchebest C., and Pullman A. Experimental and theoretical study of gramicidin P, an analog of gramicidin A with a methylamine C-terminal. FEBS Letts. 216 (1987) 11-16
    • (1987) FEBS Letts. , vol.216 , pp. 11-16
    • Trudelle, Y.1    Daumas, P.2    Heitz, F.3    Etchebest, C.4    Pullman, A.5
  • 130
    • 0026747636 scopus 로고
    • Gramicidin channel selectivity
    • Turano B., Pear M., and Busath D. Gramicidin channel selectivity. Biophys. J. 63 (1992) 152-161
    • (1992) Biophys. J. , vol.63 , pp. 152-161
    • Turano, B.1    Pear, M.2    Busath, D.3
  • 131
    • 0015027073 scopus 로고
    • The gramicidin A transmembrane channel: A proposed π(l,d) helix
    • Urry D.W. The gramicidin A transmembrane channel: A proposed π(l,d) helix. Proc. Natl. Acad. Sci. USA 68 (1972) 672-676
    • (1972) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 672-676
    • Urry, D.W.1
  • 132
    • 0028210368 scopus 로고
    • The conformation of linear gramicidin is sequence dependent: A monolayer and infrared study
    • Van Mau N., Bonnet B., Benayad A., and Heitz F. The conformation of linear gramicidin is sequence dependent: A monolayer and infrared study. Eur. Biophys. J. 22 (1994) 447-452
    • (1994) Eur. Biophys. J. , vol.22 , pp. 447-452
    • Van Mau, N.1    Bonnet, B.2    Benayad, A.3    Heitz, F.4
  • 134
    • 0016776797 scopus 로고
    • Simultaneous fluorescence and conductance studies of planar bilayer membranes containing a highly active and fluorescent analog of gramicidin A
    • Veatch W.R., Mathies R., Eisenberg, and Stryer L. Simultaneous fluorescence and conductance studies of planar bilayer membranes containing a highly active and fluorescent analog of gramicidin A. J. Mol. Biol. 99 (1975) 75-92
    • (1975) J. Mol. Biol. , vol.99 , pp. 75-92
    • Veatch, W.R.1    Mathies, R.2    Eisenberg3    Stryer, L.4
  • 135
    • 84986533210 scopus 로고
    • Theoretical conformational analysis of the gramicidin A transmembrane channel. I. Helix sense and energetics of head-to-head dimerization
    • Venkatachalam C.M., and Urry D.W. Theoretical conformational analysis of the gramicidin A transmembrane channel. I. Helix sense and energetics of head-to-head dimerization. J. Comp. Chem. 4 (1983) 461-469
    • (1983) J. Comp. Chem. , vol.4 , pp. 461-469
    • Venkatachalam, C.M.1    Urry, D.W.2
  • 136
    • 0026051772 scopus 로고
    • Synthesis of acylated gramicidins and the influence of acylation on the interfacial properties and conformational behaviour of gramicidin A
    • Vogt T.B.C., Killian J.A., Demel R.A., and De Kruijff B. Synthesis of acylated gramicidins and the influence of acylation on the interfacial properties and conformational behaviour of gramicidin A. Biochim. Biophys. Acta 1069 (1991) 157-164
    • (1991) Biochim. Biophys. Acta , vol.1069 , pp. 157-164
    • Vogt, T.B.C.1    Killian, J.A.2    Demel, R.A.3    De Kruijff, B.4
  • 137
    • 0026775927 scopus 로고
    • Influence of acylation on channel characteristics of gramicidin A
    • Vogt T.B.C., Killian J.A., De Kruijff B., and Andersen O.S. Influence of acylation on channel characteristics of gramicidin A. Biochemistry 31 (1992) 7320-7324
    • (1992) Biochemistry , vol.31 , pp. 7320-7324
    • Vogt, T.B.C.1    Killian, J.A.2    De Kruijff, B.3    Andersen, O.S.4
  • 138
    • 0021323579 scopus 로고
    • Ion-bound forms of the gramicidin A transmembrane channel
    • Wallace B.A. Ion-bound forms of the gramicidin A transmembrane channel. Biophys. J. 45 (1984) 114-116
    • (1984) Biophys. J. , vol.45 , pp. 114-116
    • Wallace, B.A.1
  • 139
    • 0022640540 scopus 로고
    • Structure of gramicidin A
    • Wallace B.A. Structure of gramicidin A. Biophys. J. 49 (1986) 295-307
    • (1986) Biophys. J. , vol.49 , pp. 295-307
    • Wallace, B.A.1
  • 141
    • 0026494358 scopus 로고
    • Crystallographic studies of a transmembrane ion channel, gramicidin A
    • Wallace B.A. Crystallographic studies of a transmembrane ion channel, gramicidin A. Prog. Biophys. Molec. Biol. 57 (1992) 59-69
    • (1992) Prog. Biophys. Molec. Biol. , vol.57 , pp. 59-69
    • Wallace, B.A.1
  • 142
    • 0001093275 scopus 로고
    • The use of single-wavelength anomalous scattering to solve the crystal structure of a gramicidin A/caesium chloride complex
    • Wallace B.A., Hendrickson W.A., and Ravikumar K. The use of single-wavelength anomalous scattering to solve the crystal structure of a gramicidin A/caesium chloride complex. Acta Cryst. B46 (1990) 440-446
    • (1990) Acta Cryst. , vol.B46 , pp. 440-446
    • Wallace, B.A.1    Hendrickson, W.A.2    Ravikumar, K.3
  • 143
    • 0024281633 scopus 로고
    • The gramicidin pore: Crystal structure of a caesium complex
    • Wallace B.A., and Ravikumar K. The gramicidin pore: Crystal structure of a caesium complex. Science 241 (1988) 182-187
    • (1988) Science , vol.241 , pp. 182-187
    • Wallace, B.A.1    Ravikumar, K.2
  • 144
    • 0019852927 scopus 로고
    • Conformation of gramicidin A in phospholipid vesicles: Circular dichroism studies of effects of ion binding, chemical modification, and lipid structure
    • Wallace B.A., Veatch W.R., and Blout E.R. Conformation of gramicidin A in phospholipid vesicles: Circular dichroism studies of effects of ion binding, chemical modification, and lipid structure. Biochemistry 20 (1981) 5754-5760
    • (1981) Biochemistry , vol.20 , pp. 5754-5760
    • Wallace, B.A.1    Veatch, W.R.2    Blout, E.R.3
  • 148
    • 0026499150 scopus 로고
    • Gramicidin-lipid interactions induce specific tryptophan side chain conformations
    • Woolley G.A., Dunn A., and Wallace B.A. Gramicidin-lipid interactions induce specific tryptophan side chain conformations. Biochem. Soc. Trans. 20 (1992) 864-867
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 864-867
    • Woolley, G.A.1    Dunn, A.2    Wallace, B.A.3
  • 149
    • 0026754487 scopus 로고
    • Model ion channels: gramicidin and alamethicin
    • Woolley G.A., and Wallace B.A. Model ion channels: gramicidin and alamethicin. J. Membr. Biol. 129 (1992) 109-136
    • (1992) J. Membr. Biol. , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 150
    • 0002314328 scopus 로고
    • Membrane protein structure: lessons from gramicidin
    • White S.H. (Ed), Oxford University Press, Sunderland, MA
    • Woolley G.A., and Wallace B.A. Membrane protein structure: lessons from gramicidin. In: White S.H. (Ed). Membrane Protein Structure: Experimental Approaches (1994), Oxford University Press, Sunderland, MA 313-334
    • (1994) Membrane Protein Structure: Experimental Approaches , pp. 313-334
    • Woolley, G.A.1    Wallace, B.A.2
  • 151
    • 0026738754 scopus 로고
    • A conformational rearrangement in gramicidin A: From a double-stranded left-handed helix to a single-stranded right-handed helix
    • Zhang Z., Pascal S.M., and Cross T.A. A conformational rearrangement in gramicidin A: From a double-stranded left-handed helix to a single-stranded right-handed helix. Biochemistry 31 (1992) 8822-8828
    • (1992) Biochemistry , vol.31 , pp. 8822-8828
    • Zhang, Z.1    Pascal, S.M.2    Cross, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.