메뉴 건너뛰기




Volumn 1757, Issue 8, 2006, Pages 876-885

Et tu, Grotthuss! and other unfinished stories

Author keywords

Membrane; Protein; Proton current; Proton transfer; Single ion channel; Water

Indexed keywords

1,3 DIOXOLANE DERIVATIVE; GRAMICIDIN; HYDROGEN; ION CHANNEL; PROTEIN; WATER;

EID: 33749043747     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2005.12.001     Document Type: Review
Times cited : (534)

References (76)
  • 1
    • 0002036605 scopus 로고
    • Sur la décomposition de l'eau et des corps q'uelle tient en dissolution à l'aide de l'électricité galvanique
    • Grotthuss C.J.T. Sur la décomposition de l'eau et des corps q'uelle tient en dissolution à l'aide de l'électricité galvanique. Ann. Chim. LVIII (1806) 54-74
    • (1806) Ann. Chim. , vol.LVIII , pp. 54-74
    • Grotthuss, C.J.T.1
  • 2
    • 33749070766 scopus 로고    scopus 로고
    • http://www.bajorusajunga.lt/en/grotthuss.html.
  • 3
    • 33749041460 scopus 로고    scopus 로고
    • J.Al. Krikštopaitis, In the wake of Volta's challenge: the eletrolysis theory of Theodor Grotthuss, 1805. Pavia Project Physics, Volta and His Influence on Physics, 2003.
  • 4
    • 33749069880 scopus 로고    scopus 로고
    • M. Faraday, Experimental Research in Electricity. Vol I, paragraphs 499 and 515, 1849. The Project Guttenberg (http://library.beau.org/gutenberg/1/4/9/8/14986/14986.txt).
  • 9
    • 33749061255 scopus 로고    scopus 로고
    • M. Planck, Das Princip der Erhaltung der Energie. Druck und Verlag von B.G. Teubner, Leipzig, 1887.
  • 10
    • 0000590116 scopus 로고
    • Notiz über ionengeschwindigkeiten
    • Danneel V.H. Notiz über ionengeschwindigkeiten. Z. Elektrochem. 11 (1905) 249-252
    • (1905) Z. Elektrochem. , vol.11 , pp. 249-252
    • Danneel, V.H.1
  • 11
    • 0001828501 scopus 로고
    • Proton solvation and proton transfer processes in solution
    • Bockris J.O.M., and Conway B.E. (Eds), Butterworth, London
    • Conway B.E. Proton solvation and proton transfer processes in solution. In: Bockris J.O.M., and Conway B.E. (Eds). Modern Aspects of Electrochemistry vol. 3 (1964), Butterworth, London 43-148
    • (1964) Modern Aspects of Electrochemistry , vol.3 , pp. 43-148
    • Conway, B.E.1
  • 12
    • 0040472558 scopus 로고
    • Proton solvation and proton transfer in chemical and electrochemical processes
    • Conway B.E., Bockris J.O.M., and Yeager E. (Eds), Plenum Press, New York
    • Lengyel S., and Conway B.E. Proton solvation and proton transfer in chemical and electrochemical processes. In: Conway B.E., Bockris J.O.M., and Yeager E. (Eds). Comprehensive Treatise of Electrochemistry (1983), Plenum Press, New York 339-398
    • (1983) Comprehensive Treatise of Electrochemistry , pp. 339-398
    • Lengyel, S.1    Conway, B.E.2
  • 14
    • 0000973004 scopus 로고
    • Theorie der beweglichkeiten des wasserstoff- und hydroxylions in wässriger lösung
    • Hückel H.E. Theorie der beweglichkeiten des wasserstoff- und hydroxylions in wässriger lösung. Z. Elektrochem. 34 (1928) 546-562
    • (1928) Z. Elektrochem. , vol.34 , pp. 546-562
    • Hückel, H.E.1
  • 15
    • 0346735076 scopus 로고
    • A theory of water and ionic solution, with particular reference to hydrogen and hydroxyl ions
    • Bernal J.D., and Fowler R.H. A theory of water and ionic solution, with particular reference to hydrogen and hydroxyl ions. J. Chem. Phys. 1 (1933) 515-548
    • (1933) J. Chem. Phys. , vol.1 , pp. 515-548
    • Bernal, J.D.1    Fowler, R.H.2
  • 16
    • 0345613372 scopus 로고
    • Molecular mechanisms for proton transport in membranes
    • Nagle J.F., and Morowitz H.J. Molecular mechanisms for proton transport in membranes. Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 298-302
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 298-302
    • Nagle, J.F.1    Morowitz, H.J.2
  • 17
    • 2242418317 scopus 로고    scopus 로고
    • Hydrogen bonds, water rotation and proton mobility
    • Agmon N. Hydrogen bonds, water rotation and proton mobility. J. Chim. Phys. 93 (1996) 1714-1736
    • (1996) J. Chim. Phys. , vol.93 , pp. 1714-1736
    • Agmon, N.1
  • 19
    • 0034614072 scopus 로고    scopus 로고
    • The mechanism of hydrated proton transfer in water
    • Day T.J.F., Schmitt U.W., and Voth G.A. The mechanism of hydrated proton transfer in water. J. Am. Chem. Soc. 122 (2000) 12027-12028
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 12027-12028
    • Day, T.J.F.1    Schmitt, U.W.2    Voth, G.A.3
  • 20
    • 5944238344 scopus 로고    scopus 로고
    • The quantum dynamics of an excess proton in water
    • Voth LobaughG.A. The quantum dynamics of an excess proton in water. J. Chem. Phys. 104 (1996) 2056-2069
    • (1996) J. Chem. Phys. , vol.104 , pp. 2056-2069
    • Voth, LobaughG.A.1
  • 21
    • 22944484741 scopus 로고    scopus 로고
    • A bond-order analysis of the mechanism for hydrated proton mobility in liquid water
    • Lapid H., Agmon N., Petersen M.K., and Voth G.A. A bond-order analysis of the mechanism for hydrated proton mobility in liquid water. J. Chem. Phys. 122 (2005) 014506
    • (2005) J. Chem. Phys. , vol.122 , pp. 014506
    • Lapid, H.1    Agmon, N.2    Petersen, M.K.3    Voth, G.A.4
  • 22
    • 1942504857 scopus 로고    scopus 로고
    • Theory and simulation of proton-coupled electron transfer, hydrogen atom transfer, and proton translocation in proteins
    • Cukier R.I. Theory and simulation of proton-coupled electron transfer, hydrogen atom transfer, and proton translocation in proteins. Biochem. Biophys. Acta 1655 (2004) 37-44
    • (2004) Biochem. Biophys. Acta , vol.1655 , pp. 37-44
    • Cukier, R.I.1
  • 23
    • 0034640371 scopus 로고    scopus 로고
    • The mechanism of proton transfer: an outline
    • Krishtalik L.I. The mechanism of proton transfer: an outline. Biochim. Biophys. Acta 1458 (2000) 6-27
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 6-27
    • Krishtalik, L.I.1
  • 24
    • 0002339456 scopus 로고    scopus 로고
    • The isotope substitution effect on the hydrated proton
    • Schmitt U.W., and Voth G.A. The isotope substitution effect on the hydrated proton. Chem. Phys. Lett. 329 (2000) 36-41
    • (2000) Chem. Phys. Lett. , vol.329 , pp. 36-41
    • Schmitt, U.W.1    Voth, G.A.2
  • 25
    • 0034029250 scopus 로고    scopus 로고
    • Proton mobilities in water and in different stereoisomers of covalently linked gramicidin A channels
    • Cukierman S. Proton mobilities in water and in different stereoisomers of covalently linked gramicidin A channels. Biophys. J. 78 (2000) 1825-1834
    • (2000) Biophys. J. , vol.78 , pp. 1825-1834
    • Cukierman, S.1
  • 26
    • 0032706238 scopus 로고    scopus 로고
    • The conduction of protons in different stereoisomers of dioxolane-linked gramicidin A channels
    • Quigley E.P., Quigley P., Crumrine D.S., and Cukierman S. The conduction of protons in different stereoisomers of dioxolane-linked gramicidin A channels. Biophys. J. 77 (1999) 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
    • 0000850642 scopus 로고
    • Determination of ionic mobilities in aqueous hydrochloric acid solutions of different concentration at various temperatures
    • Lengyel S., Giber J., and Tamás J. Determination of ionic mobilities in aqueous hydrochloric acid solutions of different concentration at various temperatures. Acta Chim. Hung. 32 (1962) 429-436
    • (1962) Acta Chim. Hung. , vol.32 , pp. 429-436
    • Lengyel, S.1    Giber, J.2    Tamás, J.3
  • 28
    • 0015005056 scopus 로고
    • Proton transfer conduction in aqueous solution: Part I. Conductance of concentrated aqueous alkali metal hydroxide solutions at elevated temperatures and pressures
    • Lown D.A., and Thirsk H.R. Proton transfer conduction in aqueous solution: Part I. Conductance of concentrated aqueous alkali metal hydroxide solutions at elevated temperatures and pressures. Trans. Faraday Soc. 67 (1971) 132-148
    • (1971) Trans. Faraday Soc. , vol.67 , pp. 132-148
    • Lown, D.A.1    Thirsk, H.R.2
  • 29
    • 0004077163 scopus 로고
    • Proton transfer conduction in aqueous solution. Part 2-Effect of pressure on the electrical conductivity of concentrated orthophosphoric acid in water at 25 °C
    • Lown D.A., and Thirsk H.R. Proton transfer conduction in aqueous solution. Part 2-Effect of pressure on the electrical conductivity of concentrated orthophosphoric acid in water at 25 °C. Trans. Faraday Soc. 67 (1971) 149-152
    • (1971) Trans. Faraday Soc. , vol.67 , pp. 149-152
    • Lown, D.A.1    Thirsk, H.R.2
  • 30
    • 0001519635 scopus 로고
    • The conductance of hydrochloric acid in aqueous solutions from 5° to 65°
    • Owen B.B., and Sweeton F.H. The conductance of hydrochloric acid in aqueous solutions from 5° to 65°. J. Am. Chem. Soc. 63 (1941) 2811-2817
    • (1941) J. Am. Chem. Soc. , vol.63 , pp. 2811-2817
    • Owen, B.B.1    Sweeton, F.H.2
  • 31
    • 0037458056 scopus 로고    scopus 로고
    • Kinetic isotope effects of proton transfer in aqueous methanol containing solutions, and in gramicidin channels
    • Chernyshev A., Pomès R., and Cukierman S. Kinetic isotope effects of proton transfer in aqueous methanol containing solutions, and in gramicidin channels. Biophys. Chem. 103 (2003) 179-190
    • (2003) Biophys. Chem. , vol.103 , pp. 179-190
    • Chernyshev, A.1    Pomès, R.2    Cukierman, S.3
  • 32
    • 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 (1996) 19-39
    • (1996) Biophys. J. , vol.71 , pp. 19-39
    • Pomès, R.1    Roux, B.2
  • 33
    • 0035807787 scopus 로고    scopus 로고
    • Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors
    • Adelroth P., Paddock M.L., Tehrani A., Beatty J.T., Feher G., and Okamura M.Y. Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors. Biochemistry 40 (2001) 14538-14546
    • (2001) Biochemistry , vol.40 , pp. 14538-14546
    • Adelroth, P.1    Paddock, M.L.2    Tehrani, A.3    Beatty, J.T.4    Feher, G.5    Okamura, M.Y.6
  • 34
    • 0029032587 scopus 로고
    • Interruption of the water chain in the reaction center from rb. sphaeroides reduces the rate of the proton uptake and of the second electron transfer to Q_B
    • Baciou L., and Michel H. Interruption of the water chain in the reaction center from rb. sphaeroides reduces the rate of the proton uptake and of the second electron transfer to Q_B. Biochem. 34 (1995) 7967-7972
    • (1995) Biochem. , vol.34 , pp. 7967-7972
    • Baciou, L.1    Michel, H.2
  • 35
    • 0032848775 scopus 로고    scopus 로고
    • In Rhodobacter sphaeroides reaction centers, mutation of proline L209 to aromatic residues in the vicinity of a water channel alters the dynamic coupling between electron and proton transfer processes
    • Tandori J., Sebban P., Michel H., and Baciou L. In Rhodobacter sphaeroides reaction centers, mutation of proline L209 to aromatic residues in the vicinity of a water channel alters the dynamic coupling between electron and proton transfer processes. Biochemistry 38 (1999) 13179-13187
    • (1999) Biochemistry , vol.38 , pp. 13179-13187
    • Tandori, J.1    Sebban, P.2    Michel, H.3    Baciou, L.4
  • 36
    • 0035846967 scopus 로고    scopus 로고
    • Structure of cytochrome c oxidase: a comparison of the bacterial and mitochondrial enzymes
    • Abramson J., Ek-Svensson M., Byrne B., and Iwata S. Structure of cytochrome c oxidase: a comparison of the bacterial and mitochondrial enzymes. Biochem. Biophys. Acta 1544 (2001) 1-9
    • (2001) Biochem. Biophys. Acta , vol.1544 , pp. 1-9
    • Abramson, J.1    Ek-Svensson, M.2    Byrne, B.3    Iwata, S.4
  • 38
    • 3242763877 scopus 로고    scopus 로고
    • Redox-driven membrane-bound proton pumps
    • Brzezinski P. Redox-driven membrane-bound proton pumps. Trends Biochem. Sci. 29 (2004) 380-387
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 380-387
    • Brzezinski, P.1
  • 39
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
    • Iwata S., Ostermeier C., Ludwig B., and Michel H. Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans. Nature 376 (1995) 660-669
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 40
    • 0034643829 scopus 로고    scopus 로고
    • Localized control of proton transfer through the D-pathway in cytochrome c oxidase: application of the proton-inventory technique
    • Karpefors M., Adelroth P., and Brzezinski P. Localized control of proton transfer through the D-pathway in cytochrome c oxidase: application of the proton-inventory technique. Biochemistry 39 (2000) 6850-6856
    • (2000) Biochemistry , vol.39 , pp. 6850-6856
    • Karpefors, M.1    Adelroth, P.2    Brzezinski, P.3
  • 42
    • 0034640504 scopus 로고    scopus 로고
    • Proton pumping by cytochrome oxidase: progress, problems, and postulates
    • Zaslavsky D., and Gennis R.B. Proton pumping by cytochrome oxidase: progress, problems, and postulates. Biochim. Biophys. Acta 1458 (2000) 164-179
    • (2000) Biochim. Biophys. Acta , vol.1458 , pp. 164-179
    • Zaslavsky, D.1    Gennis, R.B.2
  • 44
    • 0037466289 scopus 로고    scopus 로고
    • Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M1, M2, and M2' intermediates of the photocycle
    • Lanyi J.K., and Schobert B. Mechanism of proton transport in bacteriorhodopsin from crystallographic structures of the K, L, M1, M2, and M2' intermediates of the photocycle. J. Mol. Biol. 328 (2003) 439-450
    • (2003) J. Mol. Biol. , vol.328 , pp. 439-450
    • Lanyi, J.K.1    Schobert, B.2
  • 45
    • 0038649076 scopus 로고    scopus 로고
    • Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base
    • Schobert B., Brown L.S., and Lanyi J.K. Crystallographic structures of the M and N intermediates of bacteriorhodopsin: assembly of a hydrogen-bonded chain of water molecules between Asp-96 and the retinal Schiff base. J. Mol. Bio. 330 (2003) 553-570
    • (2003) J. Mol. Bio. , vol.330 , pp. 553-570
    • Schobert, B.1    Brown, L.S.2    Lanyi, J.K.3
  • 46
    • 0032484201 scopus 로고    scopus 로고
    • Biological hydrogen production: not so elementary
    • Adams M.W.W., and Stiefel E.I. Biological hydrogen production: not so elementary. Science 282 (1998) 1842-1843
    • (1998) Science , vol.282 , pp. 1842-1843
    • Adams, M.W.W.1    Stiefel, E.I.2
  • 47
    • 0003723366 scopus 로고    scopus 로고
    • Cammack R.M., Frey M., and Robson R. (Eds), Taylor and Francis, London
    • In: Cammack R.M., Frey M., and Robson R. (Eds). Hydrogen as a Fuel. Learning from Nature (2001), Taylor and Francis, London
    • (2001) Hydrogen as a Fuel. Learning from Nature
  • 48
    • 0032483966 scopus 로고    scopus 로고
    • X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 Å angstrom resolution
    • Peters J.W., Lanzilotta W.N., Lemon B.J., and Seefeldt L.C. X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 Å angstrom resolution. Science 282 (1998) 1853-1858
    • (1998) Science , vol.282 , pp. 1853-1858
    • Peters, J.W.1    Lanzilotta, W.N.2    Lemon, B.J.3    Seefeldt, L.C.4
  • 49
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • DeCoursey T.E. Voltage-gated proton channels and other proton transfer pathways. Physiol. Rev. 83 (2003) 475-579
    • (2003) Physiol. Rev. , vol.83 , pp. 475-579
    • DeCoursey, T.E.1
  • 50
    • 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 AL., and Ovchinnikov Y.A. Proton NMR study of gramicidin A transmembrane ion channel. Head-to-head right handed, single stranded helices. FEBS Lett. 186 (1985) 168-174
    • (1985) FEBS Lett. , vol.186 , pp. 168-174
    • Arseniev, A.S.1    Barsukov, I.L.2    Bystrov, V.F.3    Lonize, AL.4    Ovchinnikov, Y.A.5
  • 51
    • 0031574382 scopus 로고    scopus 로고
    • High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived constraints
    • Ketchem R.R., Roux B., and Cross T.A. High-resolution polypeptide structure in a lamellar phase lipid environment from solid state NMR derived constraints. Structure 5 (1997) 1655-1669
    • (1997) Structure , vol.5 , pp. 1655-1669
    • Ketchem, R.R.1    Roux, B.2    Cross, T.A.3
  • 53
    • 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. Biochem. Biophys. Acta 274 (1972) 294-312
    • (1972) Biochem. Biophys. Acta , vol.274 , pp. 294-312
    • Hladky, S.B.1    Haydon, D.A.2
  • 54
    • 0002535080 scopus 로고
    • Water movement through lipid bilayers, pores, and plasma membrane
    • John Wiley, New York
    • Finkelstein A. Water movement through lipid bilayers, pores, and plasma membrane. Theory and Reality (1987), John Wiley, New York
    • (1987) Theory and Reality
    • Finkelstein, A.1
  • 55
    • 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., and Hautman J.M. Number of water molecules coupled to the transport of sodium, potassium, and hydrogen ions via gramicidin nonactin or valinomycin. Biochem. Biophys. Acta 512 (1978) 436-451
    • (1978) Biochem. Biophys. Acta , vol.512 , pp. 436-451
    • Levitt, D.G.1    Elias, S.R.2    Hautman, J.M.3
  • 56
    • 0031806428 scopus 로고    scopus 로고
    • Streaming potentials in gramicidin channels measured with ion selective electrodes
    • Tripathi S., and Hladky S.B. Streaming potentials in gramicidin channels measured with ion selective electrodes. Biophys. J. 74 (1998) 2912-2917
    • (1998) Biophys. J. , vol.74 , pp. 2912-2917
    • Tripathi, S.1    Hladky, S.B.2
  • 57
    • 0035073446 scopus 로고    scopus 로고
    • Covalently linked gramicidin channels: effects of linker hydrophobicity and alkaline metals on different stereoisomers
    • Armstrong K.M., Quigley E.P., Quigley P., Crumrine D.S., and Cukierman S. Covalently linked gramicidin channels: effects of linker hydrophobicity and alkaline metals on different stereoisomers. Biophys. J. 80 (2001) 1810-1818
    • (2001) Biophys. J. , vol.80 , pp. 1810-1818
    • Armstrong, K.M.1    Quigley, E.P.2    Quigley, P.3    Crumrine, D.S.4    Cukierman, S.5
  • 58
    • 0017354373 scopus 로고
    • The action of a carbonsuboxide dimerized gramicidin A on lipid bilayer membranes
    • Bamberg E., and Janko K. The action of a carbonsuboxide dimerized gramicidin A on lipid bilayer membranes. Biochem. Biophys. Acta 465 (1977) 486-499
    • (1977) Biochem. Biophys. Acta , vol.465 , pp. 486-499
    • Bamberg, E.1    Janko, K.2
  • 59
    • 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., and Crumrine D.S. Proton conduction in gramicidin A and in its dioxolane-linked dimer in different lipid bilayers. Biophys. J. 73 (1997) 2489-2502
    • (1997) Biophys. J. , vol.73 , pp. 2489-2502
    • Cukierman, S.1    Quigley, E.P.2    Crumrine, D.S.3
  • 61
    • 0019449066 scopus 로고
    • The dependence of the conductance and lifetime of gramicidin channels on the thickness and tension of lipid bilayers
    • Rudnev V.S., Ermishkin L.N., Fonina L.A., and Rovin Yu.G. The dependence of the conductance and lifetime of gramicidin channels on the thickness and tension of lipid bilayers. Biochem. Biophys. Acta 642 (1981) 196-202
    • (1981) Biochem. Biophys. Acta , vol.642 , pp. 196-202
    • Rudnev, V.S.1    Ermishkin, L.N.2    Fonina, L.A.3    Rovin, Yu.G.4
  • 62
    • 0028108503 scopus 로고
    • A molecular dynamics study of gating in dioxolane-linked gramicidin A channels
    • Crouzy S., Woolf T.B., and Roux B. A molecular dynamics study of gating in dioxolane-linked gramicidin A channels. Biophys. J. 67 (1994) 1370-1386
    • (1994) Biophys. J. , vol.67 , pp. 1370-1386
    • Crouzy, S.1    Woolf, T.B.2    Roux, B.3
  • 64
    • 0037304680 scopus 로고    scopus 로고
    • Theoretical study of the structure and dynamic fluctuations of dioxolane-linked gramicidin channels
    • Yu C.H., Cukierman S., and Pomès R. Theoretical study of the structure and dynamic fluctuations of dioxolane-linked gramicidin channels. Biophys. J. 84 (2003) 816-831
    • (2003) Biophys. J. , vol.84 , pp. 816-831
    • Yu, C.H.1    Cukierman, S.2    Pomès, R.3
  • 65
    • 45849155018 scopus 로고    scopus 로고
    • Saturation of conductance in single ion channels: the blocking effect of the near reaction field
    • Nadler B., Schuss Z., Hollerbach U., and Eisenberg R.S. Saturation of conductance in single ion channels: the blocking effect of the near reaction field. Phys. Rev., E 70 (2004) 05192-1-05192-11
    • (2004) Phys. Rev., E , vol.70
    • Nadler, B.1    Schuss, Z.2    Hollerbach, U.3    Eisenberg, R.S.4
  • 66
    • 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. Memb. Biol. 39 (1981) 155-171
    • (1981) J. Memb. Biol. , vol.39 , pp. 155-171
    • Finkelstein, A.1    Andersen, O.S.2
  • 68
    • 0018393094 scopus 로고
    • A study of gramicidin using deuterium oxide
    • Tredgold R.H., and Jones R. A study of gramicidin using deuterium oxide. Biochim. Biophys. Acta 550 (1979) 543-545
    • (1979) Biochim. Biophys. Acta , vol.550 , pp. 543-545
    • Tredgold, R.H.1    Jones, R.2
  • 69
    • 0036221414 scopus 로고    scopus 로고
    • Thermodynamic view of activation energies of proton transfer in various gramicidin A channels
    • Chernyshev A., and Cukierman S. Thermodynamic view of activation energies of proton transfer in various gramicidin A channels. Biophys. J. 82 (2002) 182-192
    • (2002) Biophys. J. , vol.82 , pp. 182-192
    • Chernyshev, A.1    Cukierman, S.2
  • 70
    • 0242490603 scopus 로고    scopus 로고
    • Functional dynamics of ion channels: modulation of proton movement by conformational switches
    • Yu C.H., and Pomès R. Functional dynamics of ion channels: modulation of proton movement by conformational switches. J. Am. Chem. Soc. 125 (2003) 13890-13894
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13890-13894
    • Yu, C.H.1    Pomès, R.2
  • 72
    • 0033638375 scopus 로고    scopus 로고
    • A combined molecular dynamics and diffusion model of single proton conduction through gramicidin
    • Schumaker M.F., Pomes R., and Roux B. A combined molecular dynamics and diffusion model of single proton conduction through gramicidin. Biophys. J. 79 (2000) 2840-2847
    • (2000) Biophys. J. , vol.79 , pp. 2840-2847
    • Schumaker, M.F.1    Pomes, R.2    Roux, B.3
  • 73
    • 0033270107 scopus 로고    scopus 로고
    • Flying protons in linked gramicidin A channels
    • Cukierman S. Flying protons in linked gramicidin A channels. Isr. J. Chem. 39 (1999) 419-426
    • (1999) Isr. J. Chem. , vol.39 , pp. 419-426
    • Cukierman, S.1
  • 74
    • 0034866659 scopus 로고    scopus 로고
    • Modulation of proton transfer in the water wire of dioxolane-linked gramicidin channels by lipid membranes
    • Godoy C.M.G., and Cukierman S. Modulation of proton transfer in the water wire of dioxolane-linked gramicidin channels by lipid membranes. Biophys. J. 81 (2001) 1430-1438
    • (2001) Biophys. J. , vol.81 , pp. 1430-1438
    • Godoy, C.M.G.1    Cukierman, S.2
  • 75
    • 12344277810 scopus 로고    scopus 로고
    • Realistic simulations of proton transport along the gramicidin channel: demonstrating the importance of solvation effects
    • Braun-Sand S., Burykin A., Chu Z.T., and Warshel A. Realistic simulations of proton transport along the gramicidin channel: demonstrating the importance of solvation effects. J. Phys. Chem., B 109 (2005) 583-592
    • (2005) J. Phys. Chem., B , vol.109 , pp. 583-592
    • Braun-Sand, S.1    Burykin, A.2    Chu, Z.T.3    Warshel, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.