메뉴 건너뛰기




Volumn 75, Issue 6, 1998, Pages 2830-2844

Noncontact dipole effects on channel permeation. I. Experiments with (5F-indole)Trp13 gramicidin A channels

Author keywords

[No Author keywords available]

Indexed keywords

GRAMICIDIN A;

EID: 0031769568     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(98)77726-4     Document Type: Article
Times cited : (112)

References (76)
  • 2
    • 0020538940 scopus 로고
    • Ion movement through gramicidin a channels. Interfacial polarization effects on single-channel current measurements
    • Andersen, O. S. 1983. Ion movement through gramicidin A channels. Interfacial polarization effects on single-channel current measurements. Biophys. J. 41:135-146.
    • (1983) Biophys. J. , vol.41 , pp. 135-146
    • Andersen, O.S.1
  • 3
    • 0016739731 scopus 로고
    • Potential energy barriers to ion transport within lipid bilayers. Studies with tetraphenylborate
    • Andersen, O. S., and M. Fuchs. 1975. Potential energy barriers to ion transport within lipid bilayers. Studies with tetraphenylborate. Biophys. J. 15:795-830.
    • (1975) Biophys. J. , vol.15 , pp. 795-830
    • Andersen, O.S.1    Fuchs, M.2
  • 4
    • 0032478974 scopus 로고    scopus 로고
    • Importance of tryptophan dipoles for protein function: 5-fluorination of tryptophans in gramicidin a channels
    • Andersen, O. S., D. V. Greathouse, L. L. Providence, M. D. Becker, and R. E. Koeppe, II. 1998. Importance of tryptophan dipoles for protein function: 5-fluorination of tryptophans in gramicidin A channels. J. Am. Chem. Soc. 120:5142-5146.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5142-5146
    • Andersen, O.S.1    Greathouse, D.V.2    Providence, L.L.3    Becker, M.D.4    Koeppe R.E. II5
  • 5
    • 0026471029 scopus 로고
    • Molecular determinants of channel function
    • Andersen, O. S., and R. E. Koeppe, II. 1992. Molecular determinants of channel function. Physiol. Rev. 72:S89-S158.
    • (1992) Physiol. Rev. , vol.72
    • Andersen, O.S.1    Koeppe R.E. II2
  • 7
    • 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., D. V. Greathouse, R. E. Koeppe, II, and O. S. Andersen. 1991. Amino acid sequence modulation of gramicidin channel function: effects of tryptophan-to-phenylalanine substitutions on the single-channel conductance and duration. Biochemistry. 30:8830-8839.
    • (1991) Biochemistry , vol.30 , pp. 8830-8839
    • Becker, M.D.1    Greathouse, D.V.2    Koeppe R.E. II3    Andersen, O.S.4
  • 8
    • 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
    • Benamar, D., P. Daumas, Y. Trudelle, B. Calas, R. Bennes, and F. Heitz. 1993. 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. 22:145-150.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 145-150
    • Benamar, D.1    Daumas, P.2    Trudelle, Y.3    Calas, B.4    Bennes, R.5    Heitz, F.6
  • 11
    • 0027982642 scopus 로고
    • Dipole potentials of lipid membranes
    • Brockman, H. 1994. Dipole potentials of lipid membranes. Chem. Phys. Lipids. 73:57-79.
    • (1994) Chem. Phys. Lipids , vol.73 , pp. 57-79
    • Brockman, H.1
  • 12
    • 0027533833 scopus 로고
    • The use of physical methods in determining gramicidin channel structure and function
    • Busath, D. D. 1993. The use of physical methods in determining gramicidin channel structure and function. Annu. Rev. Physiol. 55:473-501.
    • (1993) Annu. Rev. Physiol. , vol.55 , pp. 473-501
    • Busath, D.D.1
  • 13
    • 0019850439 scopus 로고
    • Gramicidin forms multi-state rectifying channels
    • Busath, D., and G. Szabo. 1981. Gramicidin forms multi-state rectifying channels. Nature. 294:371-373.
    • (1981) Nature , vol.294 , pp. 371-373
    • Busath, D.1    Szabo, G.2
  • 15
    • 0001988019 scopus 로고
    • Photolysis of gramicidin a channels in lipid bilayers
    • Busath, D. D., and R. C. Waldbillig. 1983. Photolysis of gramicidin A channels in lipid bilayers. Biochim. Biophys. Acta. 736:28-38.
    • (1983) Biochim. Biophys. Acta , vol.736 , pp. 28-38
    • Busath, D.D.1    Waldbillig, R.C.2
  • 16
    • 0031910472 scopus 로고    scopus 로고
    • The absorption of phloretin to lipid monolayers and bilayers cannot be explained by Langmuir adsorption isotherms alone
    • Cseh, R., and R. Benz. 1998. The absorption of phloretin to lipid monolayers and bilayers cannot be explained by Langmuir adsorption isotherms alone. Biophys. J. 74:1399-1408.
    • (1998) Biophys. J. , vol.74 , pp. 1399-1408
    • Cseh, R.1    Benz, R.2
  • 18
    • 0024589357 scopus 로고
    • Gramicidin a analogs: Influence of the substitution of the tryptophans by naphthylalanines
    • Daumas, P., F. Heitz, L. Ranjalahy-Rasoloarijao, and R. Lazaro. 1989. Gramicidin A analogs: influence of the substitution of the tryptophans by naphthylalanines. Biochimie. 71:77-81.
    • (1989) Biochimie , vol.71 , pp. 77-81
    • Daumas, P.1    Heitz, F.2    Ranjalahy-Rasoloarijao, L.3    Lazaro, R.4
  • 20
    • 0019885221 scopus 로고
    • The thickness of monoolein lipid bilayers as determined from reflectance measurements
    • Dilger, J. P. 1981. The thickness of monoolein lipid bilayers as determined from reflectance measurements. Biochim. Biophys. Acta. 645:357-363.
    • (1981) Biochim. Biophys. Acta , vol.645 , pp. 357-363
    • Dilger, J.P.1
  • 22
    • 0011159265 scopus 로고
    • Electrical behavior of single-filing channels
    • W. Chang, I. Tasaki, W. Adelman, and R. Leuchtag, editors. Plenum, New York
    • Eisenman, G., J. Sandblom, and J. Hägglund. 1983. Electrical behavior of single-filing channels. In Structure and Function in Excitable Cells. W. Chang, I. Tasaki, W. Adelman, and R. Leuchtag, editors. Plenum, New York. 383-413.
    • (1983) Structure and Function in Excitable Cells , pp. 383-413
    • Eisenman, G.1    Sandblom, J.2    Hägglund, J.3
  • 26
    • 0022670331 scopus 로고
    • The membrane dipole potential in a total membrane potential model. Applications to hydrophobic ion interactions with membranes
    • Flewelling, R. F., and W. L. Hubbell. 1986. The membrane dipole potential in a total membrane potential model. Applications to hydrophobic ion interactions with membranes. Biophys. J. 49:541-552.
    • (1986) Biophys. J. , vol.49 , pp. 541-552
    • Flewelling, R.F.1    Hubbell, W.L.2
  • 28
    • 0026635481 scopus 로고
    • Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces
    • Gawrisch, K., D. Ruston, J. Zimmerberg, V. A. Parsegian, R. P. Rand, and N. Fuller. 1992. Membrane dipole potentials, hydration forces, and the ordering of water at membrane surfaces. Biophys. J. 61:1213-1223.
    • (1992) Biophys. J. , vol.61 , pp. 1213-1223
    • Gawrisch, K.1    Ruston, D.2    Zimmerberg, J.3    Parsegian, V.A.4    Rand, R.P.5    Fuller, N.6
  • 29
    • 23544455950 scopus 로고
    • Single-salt behavior of a symmetrical 4-site channel with barriers at its middle and ends
    • Hägglund, J. V., G. Eisenman, and J. P. Sandblom. 1984. Single-salt behavior of a symmetrical 4-site channel with barriers at its middle and ends. Bull. Math. Biol. 46:41-80.
    • (1984) Bull. Math. Biol. , vol.46 , pp. 41-80
    • Hägglund, J.V.1    Eisenman, G.2    Sandblom, J.P.3
  • 30
    • 85030341785 scopus 로고    scopus 로고
    • Direct observation of membrane mediated peptide-peptide interactions with x-ray scattering
    • Harroun, T. A., K. He, W. T. Heller, T. M. Weiss, and H. W. Huang. 1998. Direct observation of membrane mediated peptide-peptide interactions with x-ray scattering. Biophys. J. 74:A302.
    • (1998) Biophys. J. , vol.74
    • Harroun, T.A.1    He, K.2    Heller, W.T.3    Weiss, T.M.4    Huang, H.W.5
  • 31
    • 0015829732 scopus 로고
    • Surface charge, surface dipoles and membrane conductance
    • Haydon, D. A., and V. B. Myers. 1973. Surface charge, surface dipoles and membrane conductance. Biochim. Biophys. Acta. 307:429-443.
    • (1973) Biochim. Biophys. Acta , vol.307 , pp. 429-443
    • Haydon, D.A.1    Myers, V.B.2
  • 33
    • 0002545024 scopus 로고
    • Linear gramicidins: Influence of the nature of the aromatic side chains on the channel conductance
    • A. Pullman, J. Jortner, and B. Pullman, editors. Kluwer Academic, Dordrecht, Boston, and London
    • Heitz, F., P. Daumas, N. Van Mau, R. Lazaro, Y. Trudelle, C. Etchebest, and A. Pullman. 1988. Linear gramicidins: influence of the nature of the aromatic side chains on the channel conductance. In Transport Through Membranes: Carriers, Channels, and Pumps. A. Pullman, J. Jortner, and B. Pullman, editors. Kluwer Academic, Dordrecht, Boston, and London. 147-165.
    • (1988) Transport Through Membranes: Carriers, Channels, and Pumps , pp. 147-165
    • Heitz, F.1    Daumas, P.2    Van Mau, N.3    Lazaro, R.4    Trudelle, Y.5    Etchebest, C.6    Pullman, A.7
  • 34
    • 0022534474 scopus 로고
    • Analysis of the ion transfer through the channel of 9,11,13,15-phenylalanylgramicidin A
    • Heitz, F., C. Gavach, G. Spach, and Y. Trudelle. 1986. Analysis of the ion transfer through the channel of 9,11,13,15-phenylalanylgramicidin A. Biophys. Chem. 24:143-148.
    • (1986) Biophys. Chem. , vol.24 , pp. 143-148
    • Heitz, F.1    Gavach, C.2    Spach, G.3    Trudelle, Y.4
  • 35
    • 0020200286 scopus 로고
    • Single channels of 9, 11, 13, and 15-destryptophyl-phenylalanyl-gramicidin A
    • Heitz, F., G. Spach, and Y. Trudelle. 1982. Single channels of 9, 11, 13, and 15-destryptophyl-phenylalanyl-gramicidin A. Biophys. J. 40:87-89.
    • (1982) Biophys. J. , vol.40 , pp. 87-89
    • Heitz, F.1    Spach, G.2    Trudelle, Y.3
  • 36
    • 0024592239 scopus 로고
    • Single channels and surface potentials of linear gramicidins
    • Heitz, F., N. Van Mau, R. Bennes, P. Daumas, and Y. Trudelle. 1989. Single channels and surface potentials of linear gramicidins. Biochimie. 71:83-88.
    • (1989) Biochimie , vol.71 , pp. 83-88
    • Heitz, F.1    Van Mau, N.2    Bennes, R.3    Daumas, P.4    Trudelle, Y.5
  • 38
    • 0018117903 scopus 로고
    • Potassium channels as multi-ion single-file pores
    • Hille, B., and W. Schwarz. 1978. Potassium channels as multi-ion single-file pores. J. Gen. Physiol. 72:409-442.
    • (1978) J. Gen. Physiol. , vol.72 , pp. 409-442
    • Hille, B.1    Schwarz, W.2
  • 39
    • 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 D. A. Haydon. 1972. Ion transfer across lipid membranes in the presence of gramicidin A. I. Studies of the unit conductance channel. Biochim. Biophys. Acta. 274:294-312.
    • (1972) Biochim. Biophys. Acta , vol.274 , pp. 294-312
    • Hladky, S.B.1    Haydon, D.A.2
  • 40
    • 0015805546 scopus 로고
    • Membrane conductance and surface potential
    • Hladky, S. B., and D. A. Haydon. 1973. Membrane conductance and surface potential. Biochim. Biophys. Acta. 318:464-468.
    • (1973) Biochim. Biophys. Acta , vol.318 , pp. 464-468
    • Hladky, S.B.1    Haydon, D.A.2
  • 42
    • 0028787147 scopus 로고
    • Tryptophan hydrogen bonding and electrical dipole moments: Functional roles in the gramicidin channel and implications for membrane proteins
    • Hu, W., and T. A. Cross. 1995. Tryptophan hydrogen bonding and electrical dipole moments: functional roles in the gramicidin channel and implications for membrane proteins. Biochemistry. 34:14147-55.
    • (1995) Biochemistry , vol.34 , pp. 14147-14155
    • Hu, W.1    Cross, T.A.2
  • 43
    • 0028882402 scopus 로고
    • Tryptophan dynamics and structural refinement in a lipid bilayer environment: Solid state NMR of the gramicidin channel
    • Hu, W., N. D. Lazo, and T. A. Cross. 1995. Tryptophan dynamics and structural refinement in a lipid bilayer environment: solid state NMR of the gramicidin channel. Biochemistry. 34:14138-14146.
    • (1995) Biochemistry , vol.34 , pp. 14138-14146
    • Hu, W.1    Lazo, N.D.2    Cross, T.A.3
  • 44
    • 0027198547 scopus 로고
    • Tryptophans in membrane proteins: Indole ring orientations in the gramicidin channel
    • Hu, W., K.-C. Lee, and T. A. Cross. 1993. Tryptophans in membrane proteins: indole ring orientations in the gramicidin channel. Biochemistry. 32:7035-7047.
    • (1993) Biochemistry , vol.32 , pp. 7035-7047
    • Hu, W.1    Lee, K.-C.2    Cross, T.A.3
  • 45
    • 0020630499 scopus 로고
    • Electrostatic modeling of ion pores. II. Effects attributable to the membrane dipole potential
    • Jordan, P. C. 1983. Electrostatic modeling of ion pores. II. Effects attributable to the membrane dipole potential. Biophys. J. 41:189-195.
    • (1983) Biophys. J. , vol.41 , pp. 189-195
    • Jordan, P.C.1
  • 46
    • 0021358272 scopus 로고
    • The total electrostatic potential in a gramicidin channel
    • Jordan, P. C. 1984. The total electrostatic potential in a gramicidin channel. J. Membr. Biol. 78:91-102.
    • (1984) J. Membr. Biol. , vol.78 , pp. 91-102
    • Jordan, P.C.1
  • 47
    • 0031574382 scopus 로고    scopus 로고
    • High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints
    • Ketchem, R. R., B. Roux, and T. A. Cross. 1997. High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints. Structure. 5:1655-1669.
    • (1997) Structure , vol.5 , pp. 1655-1669
    • Ketchem, R.R.1    Roux, B.2    Cross, T.A.3
  • 48
    • 0023154683 scopus 로고
    • Phase separation and hexagonal HII phase formation by gramicidins A, B, and C in dioleoylphasphatidylcholine model membranes. a study on the role of the tryptophan residues
    • Killian, J. A., K. N. J. Burger, and B. De Kruijff. 1987. Phase separation and hexagonal HII phase formation by gramicidins A, B, and C in dioleoylphasphatidylcholine model membranes. A study on the role of the tryptophan residues. Biochim. Biophys. Acta. 897:269-284.
    • (1987) Biochim. Biophys. Acta , vol.897 , pp. 269-284
    • Killian, J.A.1    Burger, K.N.J.2    De Kruijff, B.3
  • 49
    • 0028045061 scopus 로고
    • Orientations of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy
    • Koeppe, R. E., II, J. A. Killian, and D. V. Greathouse. 1994. Orientations of the tryptophan 9 and 11 side chains of the gramicidin channel based on deuterium nuclear magnetic resonance spectroscopy. Biophys. J. 66:14-24.
    • (1994) Biophys. J. , vol.66 , pp. 14-24
    • Koeppe R.E. II1    Killian, J.A.2    Greathouse, D.V.3
  • 50
    • 0025017338 scopus 로고
    • Distinction between dipolar and inductive effects in modulating the conductance of gramicidin channels
    • Koeppe, R. E., J. L. Mazet, and O. S. Andersen. 1990. Distinction between dipolar and inductive effects in modulating the conductance of gramicidin channels. Biochemistry. 29:512-520.
    • (1990) Biochemistry , vol.29 , pp. 512-520
    • Koeppe, R.E.1    Mazet, J.L.2    Andersen, O.S.3
  • 51
    • 0019510367 scopus 로고
    • Resolution of linear gramicidins by preparative reversed-phase high-performance liquid chromatography
    • Koeppe, R. E., II, and L. B. Weiss. 1981. Resolution of linear gramicidins by preparative reversed-phase high-performance liquid chromatography. J. Chromatogr. 208:414-418.
    • (1981) J. Chromatogr. , vol.208 , pp. 414-418
    • Koeppe R.E. II1    Weiss, L.B.2
  • 52
    • 0032539573 scopus 로고    scopus 로고
    • Amyloid fibrils may be assembled from β-helical protofibrils
    • Lazo, N. D., and D. T. Downing. 1998. Amyloid fibrils may be assembled from β-helical protofibrils. Biochemistry. 37:1731-1735.
    • (1998) Biochemistry , vol.37 , pp. 1731-1735
    • Lazo, N.D.1    Downing, D.T.2
  • 54
    • 0027424975 scopus 로고
    • Electrostatic interactions in gramicidin channels - 3-dielectric model
    • Martínez, G., and M. Sancho. 1993. Electrostatic interactions in gramicidin channels - 3-dielectric model. Eur. Biophys. J. 22:301-307.
    • (1993) Eur. Biophys. J. , vol.22 , pp. 301-307
    • Martínez, G.1    Sancho, M.2
  • 55
    • 0029833224 scopus 로고    scopus 로고
    • Boundary conditions for single-ion diffusion
    • McGill, P., and M. F. Schumaker. 1996. Boundary conditions for single-ion diffusion. Biophys. J. 71:1723-1742.
    • (1996) Biophys. J. , vol.71 , pp. 1723-1742
    • McGill, P.1    Schumaker, M.F.2
  • 56
    • 0003466969 scopus 로고
    • Prentice-Hall, Englewood Cliffs, NJ
    • Moore, W. J. 1972. Physical Chemistry. Prentice-Hall, Englewood Cliffs, NJ.
    • (1972) Physical Chemistry
    • Moore, W.J.1
  • 57
    • 0031895461 scopus 로고    scopus 로고
    • Energetics of inclusion-induced bilayer deformations
    • Nielsen, C., M. Goulian, and O. S. Andersen. 1998. Energetics of inclusion-induced bilayer deformations. Biophys. J. 74:1966-1983.
    • (1998) Biophys. J. , vol.74 , pp. 1966-1983
    • Nielsen, C.1    Goulian, M.2    Andersen, O.S.3
  • 58
    • 0037937003 scopus 로고
    • A dipolar chain model for the electrostatics of transmembrane ion channels
    • Partenskii, M. B., M. Cai, and P. C. Jordan. 1991. A dipolar chain model for the electrostatics of transmembrane ion channels. Chem. Phys. 153: 125-131.
    • (1991) Chem. Phys. , vol.153 , pp. 125-131
    • Partenskii, M.B.1    Cai, M.2    Jordan, P.C.3
  • 59
    • 0342933118 scopus 로고
    • Transport of oppositely charged lipophilic probe ions in lipid bilayer membranes having various structures
    • Pickar, A. D., and R. Benz. 1978. Transport of oppositely charged lipophilic probe ions in lipid bilayer membranes having various structures. J. Membr. Biol. 44:353-376.
    • (1978) J. Membr. Biol. , vol.44 , pp. 353-376
    • Pickar, A.D.1    Benz, R.2
  • 61
    • 0027232024 scopus 로고
    • Ion transport in a model gramicidin channel. Free energy of the solvated right-handed dimer in a model membrane
    • Roux, B., and M. Karplus. 1993. Ion transport in a model gramicidin channel. Free energy of the solvated right-handed dimer in a model membrane. J. Am. Chem. Soc. 115:3250-3262.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 3250-3262
    • Roux, B.1    Karplus, M.2
  • 62
    • 0022638390 scopus 로고
    • Single-channel studies on linear gramicidin with altered amino acid side chains
    • Russell, E. W. B., L. B. Weiss, F. I. Navetta, R. E. Koeppe, II, and O. S. Andersen. 1986. Single-channel studies on linear gramicidin with altered amino acid side chains. Biophys. J. 49:673-686.
    • (1986) Biophys. J. , vol.49 , pp. 673-686
    • Russell, E.W.B.1    Weiss, L.B.2    Navetta, F.I.3    Koeppe R.E. II4    Andersen, O.S.5
  • 63
    • 0025862320 scopus 로고
    • Electrostatic modeling of dipole-ion interactions in gramicidin like channels
    • Sancho, M., and G. Martínez. 1991. Electrostatic modeling of dipole-ion interactions in gramicidin like channels. Biophys. J. 60:81-88.
    • (1991) Biophys. J. , vol.60 , pp. 81-88
    • Sancho, M.1    Martínez, G.2
  • 64
    • 0344141064 scopus 로고
    • Some properties of channels formed by gramicidin a and B, including their hybrid forms, in the presence of protons
    • Sandblom, J. P., R. M. Josefsson, and T. Larsson. 1990. Some properties of channels formed by gramicidin A and B, including their hybrid forms, in the presence of protons. In 10th International Biophysics Congress, Abstracts. 391.
    • (1990) 10th International Biophysics Congress, Abstracts , pp. 391
    • Sandblom, J.P.1    Josefsson, R.M.2    Larsson, T.3
  • 65
    • 0029053366 scopus 로고
    • Gramicidin tryptophans mediate formamidinium-induced channel stabilization
    • Seoh, S., and D. Busath. 1995. Gramicidin tryptophans mediate formamidinium-induced channel stabilization. Biophys. J. 68:2271-2279.
    • (1995) Biophys. J. , vol.68 , pp. 2271-2279
    • Seoh, S.1    Busath, D.2
  • 66
    • 0024389203 scopus 로고
    • Magnitude of solvation pressure depends on dipole potential
    • Simon, S. A., and T. J. McIntosh. 1989. Magnitude of solvation pressure depends on dipole potential. Proc. Natl. Acad. Sci. USA. 86:9263-9267.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9263-9267
    • Simon, S.A.1    McIntosh, T.J.2
  • 67
    • 0025103378 scopus 로고
    • Environments and conformations of tryptophan side chains of gramicidin a in phospholipid bilayers studied by Raman spectroscopy
    • Takeuchi, H., Y. Nemoto, and I. Harada. 1990. Environments and conformations of tryptophan side chains of gramicidin A in phospholipid bilayers studied by Raman spectroscopy. Biochemistry. 29:1572-1579.
    • (1990) Biochemistry , vol.29 , pp. 1572-1579
    • Takeuchi, H.1    Nemoto, Y.2    Harada, I.3
  • 69
    • 0018183022 scopus 로고
    • The kinetics of ion movements in the gramicidin channel
    • Urban, B. W., S. B. Hladky, and D. A. Haydon. 1978. The kinetics of ion movements in the gramicidin channel. Fed. Proc. 37:2628-2632.
    • (1978) Fed. Proc. , vol.37 , pp. 2628-2632
    • Urban, B.W.1    Hladky, S.B.2    Haydon, D.A.3
  • 70
    • 0019129625 scopus 로고
    • Ion movements in gramicidin pores. An example of single-file transport
    • Urban, B. W., S. B. Hladky, and D. A. Haydon. 1980. Ion movements in gramicidin pores. An example of single-file transport. Biochim. Biophys. Acta. 602:331-354.
    • (1980) Biochim. Biophys. Acta , vol.602 , pp. 331-354
    • Urban, B.W.1    Hladky, S.B.2    Haydon, D.A.3
  • 71
    • 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 D. W. Urry. 1983. Theoretical conformational analysis of the gramicidin A transmembrane channel. I. Helix sense and energetics of head-to-head dimerization. J. Comp. Chem. 4:461-469.
    • (1983) J. Comp. Chem. , vol.4 , pp. 461-469
    • Venkatachalam, C.M.1    Urry, D.W.2
  • 72
    • 0018780237 scopus 로고
    • Planar bilayer membranes from pure lipids
    • Waldbillig, R. C., and G. Szabo, 1979. Planar bilayer membranes from pure lipids. Biochim. Biophys. Acta. 557:295-305.
    • (1979) Biochim. Biophys. Acta , vol.557 , pp. 295-305
    • Waldbillig, R.C.1    Szabo, G.2
  • 73
    • 0011163268 scopus 로고
    • Experimental and quantum mechanical studies of the dipole moments of quinoline and indole
    • Weiler-Feilchenfeld, H., A. Pullman, H. Berthod, and C. Giessner-Prettre. 1970. Experimental and quantum mechanical studies of the dipole moments of quinoline and indole. J. Mol. Struct. 6:297-304.
    • (1970) J. Mol. Struct. , vol.6 , pp. 297-304
    • Weiler-Feilchenfeld, H.1    Pullman, A.2    Berthod, H.3    Giessner-Prettre, C.4
  • 74
    • 0030995981 scopus 로고    scopus 로고
    • The binding site of sodium in the gramicidin a channel: Comparison of molecular dynamics with solid-state NMR data
    • Woolf, T. B., and B. Roux. 1997. The binding site of sodium in the gramicidin A channel: comparison of molecular dynamics with solid-state NMR data. Biophys. J. 72:1930-1945.
    • (1997) Biophys. J. , vol.72 , pp. 1930-1945
    • Woolf, T.B.1    Roux, B.2
  • 75
    • 0026754487 scopus 로고
    • Model ion channels-gramicidin and alamethicin
    • Woolley, G. A., and B. A. Wallace. 1992. Model ion channels-gramicidin and alamethicin. J. Membr. Biol. 129:109-136.
    • (1992) J. Membr. Biol. , vol.129 , pp. 109-136
    • Woolley, G.A.1    Wallace, B.A.2
  • 76
    • 0027918655 scopus 로고
    • Unusual structural features in the parallel beta-helix in pectate lyases
    • Yoder, M. D., S. E. Lietzke, and F. Jurnak. 1993. Unusual structural features in the parallel beta-helix in pectate lyases. Structure. 15: 241-251.
    • (1993) Structure , vol.15 , pp. 241-251
    • Yoder, M.D.1    Lietzke, S.E.2    Jurnak, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.