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Volumn 174, Issue 3, 2000, Pages 207-212

Gating and permeation in ion channels formed by gramicidin A and its dioxolane-linked dimer in Na+ and Cs+ solutions

Author keywords

Chirality; Dioxolane; Gating; Gramicidin; Permeation; Single ion channels

Indexed keywords

1,3 DIOXOLANE DERIVATIVE; DIMER; GRAMICIDIN A; ION; ION CHANNEL;

EID: 0034176260     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002320001045     Document Type: Article
Times cited : (10)

References (38)
  • 1
    • 0019299124 scopus 로고
    • Ion movement through gramicidin A channels. On the importance of the aqueous diffusion resistance and ion-water interactions
    • Andersen, O.A., Procopio, J. 1980. Ion movement through gramicidin A channels. On the importance of the aqueous diffusion resistance and ion-water interactions. Acta Physiol. Scand. Suppl. 481:27-35
    • (1980) Acta Physiol. Scand. Suppl. , vol.481 , pp. 27-35
    • Andersen, O.A.1    Procopio, J.2
  • 2
    • 0021892874 scopus 로고
    • Proton NMR study of gramicidin A transmembrane ion channel. Head-to-head right handed, single stranded helices
    • Arseniev, A.S., Barsukov, I.L., Bystrov, V.F., Lonize, A.L., Ovchinikov, Y.A. 1985. Proton NMR study of gramicidin A transmembrane ion channel. Head-to-head right handed, single stranded helices. FEBS Lett. 186:168-174
    • (1985) FEBS Lett. , vol.186 , pp. 168-174
    • Arseniev, A.S.1    Barsukov, I.L.2    Bystrov, V.F.3    Lonize, A.L.4    Ovchinikov, Y.A.5
  • 3
    • 0017354373 scopus 로고
    • The action of a carbonsuboxide dimerized gramicidin A on lipid bilayer membranes
    • Bamberg, E., Janko, K. 1977. The action of a carbonsuboxide dimerized gramicidin A on lipid bilayer membranes. Biochim. Biophys. Acta 465:486-499
    • (1977) Biochim. Biophys. Acta , vol.465 , pp. 486-499
    • Bamberg, E.1    Janko, K.2
  • 4
    • 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. Ann. Rev. Physiol. 55:473-501
    • (1993) Ann. Rev. Physiol. , vol.55 , pp. 473-501
    • Busath, D.D.1
  • 5
    • 0028108503 scopus 로고
    • A molecular dynamics study of gating in dioxolane-linked gramicidin A channels
    • Crouzy, S., Woolf, T.B., Roux, B. 1994. A molecular dynamics study of gating in dioxolane-linked gramicidin A channels. Biophys. J. 67:1370-1386
    • (1994) Biophys. J. , vol.67 , pp. 1370-1386
    • Crouzy, S.1    Woolf, T.B.2    Roux, B.3
  • 6
    • 0033270107 scopus 로고    scopus 로고
    • Flying protons in gramicidin A channels
    • Cukierman, S. 1999. Flying protons in gramicidin A channels. Isr. J. Chem. 39:419-426
    • (1999) Isr. J. Chem. , vol.39 , pp. 419-426
    • Cukierman, S.1
  • 7
    • 0030786782 scopus 로고    scopus 로고
    • Proton conduction in gramicidin A and in its dioxolane-linked dimer in different lipid bilayers
    • Cukierman, S., Quigley, E.P., Crumrine, D.S. 1997. Proton conduction in gramicidin A and in its dioxolane-linked dimer in different lipid bilayers. Biophys. J. 73:2489-2502
    • (1997) Biophys. J. , vol.73 , pp. 2489-2502
    • Cukierman, S.1    Quigley, E.P.2    Crumrine, D.S.3
  • 8
    • 0019499785 scopus 로고
    • Water transport and ion-water interaction in the gramicidin channel
    • Dani, J.A., Levitt, D.G. 1981. Water transport and ion-water interaction in the gramicidin channel. Biophys. J. 35:501-508
    • (1981) Biophys. J. , vol.35 , pp. 501-508
    • Dani, J.A.1    Levitt, D.G.2
  • 9
    • 0033270517 scopus 로고    scopus 로고
    • An electrophysiological comparison of voltage-gated proton channels, other ion channels, and other proton channels
    • DeCoursey, T.E., Cherny, V.V. 1999. An electrophysiological comparison of voltage-gated proton channels, other ion channels, and other proton channels. Isr. J. Chem. 39:-
    • (1999) Isr. J. Chem. , vol.39
    • DeCoursey, T.E.1    Cherny, V.V.2
  • 10
    • 0017835643 scopus 로고
    • Interactions in cation permeation through the gramicidin channel. Cs, Rb, K, Na, Li, Tl, H, and effects of anion binding
    • Eisenman, G., Sandblom, J., Neher, E. 1978. Interactions in cation permeation through the gramicidin channel. Cs, Rb, K, Na, Li, Tl, H, and effects of anion binding. Biophys. J. 22:307-340
    • (1978) Biophys. J. , vol.22 , pp. 307-340
    • Eisenman, G.1    Sandblom, J.2    Neher, E.3
  • 11
    • 0002535080 scopus 로고
    • Water Movement Through Lipid Bilayers, Pores, and Plasma Membrane
    • John Wiley, New York
    • Finkelstein, A. 1987. Water Movement Through Lipid Bilayers, Pores, and Plasma Membrane. Theory and Reality. John Wiley, New York
    • (1987) Theory and Reality
    • Finkelstein, A.1
  • 12
    • 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., Andersen, O.S. 1981. The gramicidin A channel: a review of its permeability characteristics with special reference to the single-file aspect of transport. J. Membrane Biol. 39:155-171
    • (1981) J. Membrane Biol. , vol.39 , pp. 155-171
    • Finkelstein, A.1    Andersen, O.S.2
  • 13
    • 0015499206 scopus 로고
    • Ion transfer across lipid membranes in the presence of gramicidin A. I. Studies of the unit conductance channel
    • Hladky, S.B., Haydon, D.A. 1972. Ion transfer across lipid membranes in the presence of gramicidin A. I. Studies of the unit conductance channel. Biochem. Biophys. Acta 274:294-312
    • (1972) Biochem. Biophys. Acta , vol.274 , pp. 294-312
    • Hladky, S.B.1    Haydon, D.A.2
  • 14
    • 0027360175 scopus 로고
    • High resolution of gramicidin A in a lipid bilayer by solid-state NMR
    • Ketchem, R.R., Hu, W., Cross, T.A. 1993. High resolution of gramicidin A in a lipid bilayer by solid-state NMR. Science 261:1457-1460
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 15
    • 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., Roux, B., Cross, T.A. 1997. High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived orientational constraints. Struct. 5:1655-1669
    • (1997) Struct. , vol.5 , pp. 1655-1669
    • Ketchem, R.R.1    Roux, B.2    Cross, T.A.3
  • 17
    • 0017369257 scopus 로고
    • Influence of membrane thickness and ion concentration on the properties of gramicidin A channel. Autocorrelation, spectral power density, relaxation and single channel studies
    • Kolb, H.A., Bamberg, E. 1977. Influence of membrane thickness and ion concentration on the properties of gramicidin A channel. Autocorrelation, spectral power density, relaxation and single channel studies. Biochim. Biophys. Acta 464:127-141
    • (1977) Biochim. Biophys. Acta , vol.464 , pp. 127-141
    • Kolb, H.A.1    Bamberg, E.2
  • 18
    • 0001244822 scopus 로고
    • Kinetics of movement in narrow channels
    • Levitt, D.G. 1984. Kinetics of movement in narrow channels. Curr. Topics in Memb. and Transp. 21:181-197
    • (1984) Curr. Topics in Memb. and Transp. , vol.21 , pp. 181-197
    • Levitt, D.G.1
  • 19
    • 0018072320 scopus 로고
    • Number of water molecules coupled to the transport of sodium, potassium, and hydrogen ions via gramicidin, nonactin or valinomycin
    • Levitt, D.G., Elias, S.R., Hautman, J.M. 1978. Number of water molecules coupled to the transport of sodium, potassium, and hydrogen ions via gramicidin, nonactin or valinomycin. Biochim. Biophys. Acta 512:436-451
    • (1978) Biochim. Biophys. Acta , vol.512 , pp. 436-451
    • Levitt, D.G.1    Elias, S.R.2    Hautman, J.M.3
  • 20
    • 0018651927 scopus 로고
    • Interaction of permeant ions with channels activated by acetylcholine in Aplysia neurones
    • Marchais, D., Marty, A. 1979. Interaction of permeant ions with channels activated by acetylcholine in Aplysia neurones. J. Physiol. 297:9-45
    • (1979) J. Physiol. , vol.297 , pp. 9-45
    • Marchais, D.1    Marty, A.2
  • 21
    • 0021472805 scopus 로고
    • Structure and dynamics of ion transport through gramicidin A
    • Mackay, D.H.J., Berens, P.H., Wilson, K.R. 1984. Structure and dynamics of ion transport through gramicidin A. Biophys. J. 46:229-248
    • (1984) Biophys. J. , vol.46 , pp. 229-248
    • Mackay, D.H.J.1    Berens, P.H.2    Wilson, K.R.3
  • 22
    • 0022536605 scopus 로고
    • External monovalent cations that impede the closing of K channels
    • Matteson, D.R., Swenson, Jr., R.P. 1986. External monovalent cations that impede the closing of K channels. J. Gen. Physiol. 87:795-816
    • (1986) J. Gen. Physiol. , vol.87 , pp. 795-816
    • Matteson, D.R.1    Swenson R.P., Jr.2
  • 23
    • 0015499163 scopus 로고
    • Ion transfer across lipid membranes in the presence of gramicidin A
    • Myers, V.B., Haydon, D.A. 1972. Ion transfer across lipid membranes in the presence of gramicidin A. Biochim. Biophys. Acta 274:313-322
    • (1972) Biochim. Biophys. Acta , vol.274 , pp. 313-322
    • Myers, V.B.1    Haydon, D.A.2
  • 24
    • 0021279736 scopus 로고
    • Voltage-dependent calcium channels from brain incorporated into planar lipid bilayers
    • Nelson, M.T., French, R.J., Krueger, B.K. 1984. Voltage-dependent calcium channels from brain incorporated into planar lipid bilayers. Nature 308:77-80
    • (1984) Nature , vol.308 , pp. 77-80
    • Nelson, M.T.1    French, R.J.2    Krueger, B.K.3
  • 25
    • 0030011088 scopus 로고    scopus 로고
    • + translocation along the single-file water chain in the gramicidin A channel
    • + translocation along the single-file water chain in the gramicidin A channel. Biophys. J. 71:9-39
    • (1996) Biophys. J. , vol.71 , pp. 9-39
    • Pomès, R.1    Roux, B.2
  • 26
    • 0032706238 scopus 로고    scopus 로고
    • Proton permeation in different stereoisomers of gramicidin A channels
    • Quigley, E.P., Quigley, P., Crumrine, D.S., Cukierman, S. 1999. Proton permeation in different stereoisomers of gramicidin A channels. Biophys. J. 77:2479-2491
    • (1999) Biophys. J. , vol.77 , pp. 2479-2491
    • Quigley, E.P.1    Quigley, P.2    Crumrine, D.S.3    Cukierman, S.4
  • 27
    • 0031737890 scopus 로고    scopus 로고
    • Proton current attentuation by methanol in a dioxolane-linked gramicidin A dimer in different lipid bilayers
    • Quigley, E.P., Emerick, A., Crumrine, D.S., Cukierman, S. 1998. Proton current attentuation by methanol in a dioxolane-linked gramicidin A dimer in different lipid bilayers. Biophys. J. 75:2811-2820
    • (1998) Biophys. J. , vol.75 , pp. 2811-2820
    • Quigley, E.P.1    Emerick, A.2    Crumrine, D.S.3    Cukierman, S.4
  • 28
    • 0026633889 scopus 로고
    • Influence of ion occupancy and membrane deformation on gramicidin A channel stability in lipid membranes
    • Ring, A. 1992. Influence of ion occupancy and membrane deformation on gramicidin A channel stability in lipid membranes. Biophys. J. 61:1306-1315
    • (1992) Biophys. J. , vol.61 , pp. 1306-1315
    • Ring, A.1
  • 29
    • 0023821046 scopus 로고
    • Modulation of gramicidin A open channel lifetime by ion occupancy
    • Ring, A., Sandblom, J. 1988. Modulation of gramicidin A open channel lifetime by ion occupancy. Biophys. J. 53:549-559
    • (1988) Biophys. J. , vol.53 , pp. 549-559
    • Ring, A.1    Sandblom, J.2
  • 30
    • 0020239478 scopus 로고
    • Measurement of channel life time in artificial lipid membranes: Dimerization kinetics of gramicidin A
    • Ring, A., Sandblom, J. 1983. Measurement of channel life time in artificial lipid membranes: dimerization kinetics of gramicidin A. J. Membrane Biol. 16:319-337
    • (1983) J. Membrane Biol. , vol.16 , pp. 319-337
    • Ring, A.1    Sandblom, J.2
  • 31
    • 33947482744 scopus 로고
    • The structure of valine-and isoleucine-gramicidin A
    • Sarges, R., Witkop, B. 1965. The structure of valine-and isoleucine-gramicidin A. J. Am. Chem. Soc. 87:2011-2019
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2011-2019
    • Sarges, R.1    Witkop, B.2
  • 33
    • 0025072282 scopus 로고
    • Immobilizing the gate of a tartaric-acid gramicidin A hybrid channel molecule by rational design
    • Stankovic, C.J., Heinemann, S.H., Schreiber, S.L. 1990. Immobilizing the gate of a tartaric-acid gramicidin A hybrid channel molecule by rational design. J. Am. Chem. Soc. 112:3702-3704
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 3702-3704
    • Stankovic, C.J.1    Heinemann, S.H.2    Schreiber, S.L.3
  • 34
    • 0018393094 scopus 로고
    • A study of gramicidin using deuterium oxide
    • Tredgold, R.H., Jones, R. 1979. A study of gramicidin using deuterium oxide. Biochim. Biophys. Acta 550:543-545
    • (1979) Biochim. Biophys. Acta , vol.550 , pp. 543-545
    • Tredgold, R.H.1    Jones, R.2
  • 35
    • 0019129625 scopus 로고
    • Ion movements in gramicidin pores: An example of single-file transport
    • Urban, B.W., Hladky, S.B., Haydon, D.A. 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
  • 36
    • 0018759138 scopus 로고
    • Ion transport in the simplest single file pore
    • Urban, B.W., Hladky, S.B. 1979. Ion transport in the simplest single file pore. Biochim. Biophys. Acta 554:410-429
    • (1979) Biochim. Biophys. Acta , vol.554 , pp. 410-429
    • Urban, B.W.1    Hladky, S.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.