메뉴 건너뛰기




Volumn 150, Issue 1, 2005, Pages 23-40

Gramicidin structure and disposition in highly curved membranes

Author keywords

Bilayer thickness mismatch; Circular dichroism; Crystallization; Cubic phase; Fluorescence quenching; X ray diffraction

Indexed keywords

DODECYL SULFATE SODIUM; GRAMICIDIN; LIPID; MEMBRANE PROTEIN; TRIFLUOROETHANOL;

EID: 15444380710     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2004.12.007     Document Type: Article
Times cited : (51)

References (40)
  • 1
    • 84971942068 scopus 로고
    • JCPDS-International Centre for Diffraction Data round robin study of silver behenate. a possible low-angle X-ray diffraction calibration standard
    • T.N. Blanton, T.C. Huang, H. Toraya, C.R. Hubbard, S.B. Robie, D. Louer, H.E. Gobel, G. Will, R. Gilles, and T. Raftery JCPDS-International Centre for Diffraction Data round robin study of silver behenate. A possible low-angle X-ray diffraction calibration standard Powder Diffr. 10 1995 91 95
    • (1995) Powder Diffr. , vol.10 , pp. 91-95
    • Blanton, T.N.1    Huang, T.C.2    Toraya, H.3    Hubbard, C.R.4    Robie, S.B.5    Louer, D.6    Gobel, H.E.7    Will, G.8    Gilles, R.9    Raftery, T.10
  • 3
    • 0019891830 scopus 로고
    • Fluorescence quenching of model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics
    • M. Caffrey, and G.W. Feigenson Fluorescence quenching of model membranes. 3. Relationship between calcium adenosinetriphosphatase enzyme activity and the affinity of the protein for phosphatidylcholines with different acyl chain characteristics Biochemistry 20 1981 1949 1961
    • (1981) Biochemistry , vol.20 , pp. 1949-1961
    • Caffrey, M.1    Feigenson, G.W.2
  • 4
    • 0033930876 scopus 로고    scopus 로고
    • A lipid's eye view of membrane protein crystallization in mesophases
    • M. Caffrey A lipid's eye view of membrane protein crystallization in mesophases Curr. Opin. Struct. Biol. 10 2000 486 497
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 486-497
    • Caffrey, M.1
  • 5
    • 0037391107 scopus 로고    scopus 로고
    • Membrane protein crystallization
    • M. Caffrey Membrane protein crystallization J. Struct. Biol. 142 2003 108 132
    • (2003) J. Struct. Biol. , vol.142 , pp. 108-132
    • Caffrey, M.1
  • 6
    • 0033028551 scopus 로고    scopus 로고
    • Lipid composition and the lateral pressure profile in bilayers
    • R.S. Cantor Lipid composition and the lateral pressure profile in bilayers Biophys. J. 76 1999 2625 2639
    • (1999) Biophys. J. , vol.76 , pp. 2625-2639
    • Cantor, R.S.1
  • 7
    • 0031540094 scopus 로고    scopus 로고
    • Solvent effect on the conformation and far UV CD spectra of gramicidin
    • Y. Chen, and B.A. Wallace Solvent effect on the conformation and far UV CD spectra of gramicidin Biopolymers 42 1997 771 781
    • (1997) Biopolymers , vol.42 , pp. 771-781
    • Chen, Y.1    Wallace, B.A.2
  • 8
    • 0032422462 scopus 로고    scopus 로고
    • A simple mechanical mixer for small viscous samples
    • A. Cheng, B. Hummel, H. Qiu, and M. Caffrey A simple mechanical mixer for small viscous samples Chem. Phys. Lipids 95 1998 11 21
    • (1998) Chem. Phys. Lipids , vol.95 , pp. 11-21
    • Cheng, A.1    Hummel, B.2    Qiu, H.3    Caffrey, M.4
  • 10
    • 0036848784 scopus 로고    scopus 로고
    • Too hot to handle? Synchrotron X-ray damage of lipid membranes and mesophases
    • V. Cherezov, K.M. Riedl, and M. Caffrey Too hot to handle? Synchrotron X-ray damage of lipid membranes and mesophases J. Synchrotron Radiat. 9 2002 333 341
    • (2002) J. Synchrotron Radiat. , vol.9 , pp. 333-341
    • Cherezov, V.1    Riedl, K.M.2    Caffrey, M.3
  • 12
    • 0028012730 scopus 로고
    • The neutral area surface of the cubic mesophase: Location and properties
    • H. Chung, and M. Caffrey The neutral area surface of the cubic mesophase: Location and properties Biophys. J. 66 1994 377 381
    • (1994) Biophys. J. , vol.66 , pp. 377-381
    • Chung, H.1    Caffrey, M.2
  • 14
    • 0028292987 scopus 로고
    • Gramicidin A/short-chain phospholipid dispersions: Chain length dependence of gramicidin conformation and lipid organization
    • D.V. Greathouse, J.F. Hinton, K.S. Kim, and R.E. Koeppe II Gramicidin A/short-chain phospholipid dispersions: Chain length dependence of gramicidin conformation and lipid organization Biochemistry 33 1994 4291 4299
    • (1994) Biochemistry , vol.33 , pp. 4291-4299
    • Greathouse, D.V.1    Hinton, J.F.2    Kim, K.S.3    Koeppe II, R.E.4
  • 15
    • 0014441009 scopus 로고
    • Phosphatidylcholine vesicles. Formation and physical characteristics
    • C. Huang Phosphatidylcholine vesicles. Formation and physical characteristics Biochemistry 8 1969 344 352
    • (1969) Biochemistry , vol.8 , pp. 344-352
    • Huang, C.1
  • 17
    • 0043095535 scopus 로고    scopus 로고
    • Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 angstrom resolution
    • G. Katona, U. Andreasson, E.M. Landau, L.E. Andreasson, and R. Neutze Lipidic cubic phase crystal structure of the photosynthetic reaction centre from Rhodobacter sphaeroides at 2.35 angstrom resolution J. Mol. Biol. 331 2003 681 692
    • (2003) J. Mol. Biol. , vol.331 , pp. 681-692
    • Katona, G.1    Andreasson, U.2    Landau, E.M.3    Andreasson, L.E.4    Neutze, R.5
  • 18
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin a in a lipid bilayer by solid-state NMR
    • R.R. Ketchem, W. Hu, and T.A. Cross 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
  • 19
    • 0023733886 scopus 로고
    • The membrane as an environment of minimal interconversion. a circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes
    • A.J. Killian, K.U. Prasad, D. Hains, and D.W. Urry The membrane as an environment of minimal interconversion. A circular dichroism study on the solvent dependence of the conformational behavior of gramicidin in diacylphosphatidylcholine model membranes Biochemistry 27 1988 4848 4855
    • (1988) Biochemistry , vol.27 , pp. 4848-4855
    • Killian, A.J.1    Prasad, K.U.2    Hains, D.3    Urry, D.W.4
  • 20
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light driven chloride pump halorhodopsin at 1.8 angstrom resolution
    • M. Kolbe, H. Besir, L.O. Essen, and D. Oesterhelt Structure of the light driven chloride pump halorhodopsin at 1.8 angstrom resolution Science 288 2000 1390 1396
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 21
    • 0008567521 scopus 로고
    • Instrumentation of fluorescence spectroscopy
    • J.R. Lakowicz Plenum Press New York, NY
    • J.R. Lakowicz Instrumentation of fluorescence spectroscopy J.R. Lakowicz Principles of fluorescence spectroscopy 1983 Plenum Press New York, NY 19 49
    • (1983) Principles of Fluorescence Spectroscopy , pp. 19-49
    • Lakowicz, J.R.1
  • 22
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • E.M. Landau, and J.P. Rosenbusch Lipidic cubic phases: A novel concept for the crystallization of membrane proteins Proc. Natl. Acad. Sci. USA 93 1996 14532 14535
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 23
    • 0024977334 scopus 로고
    • Effect of fatty acyl chain length and structure on the lamellar gel to liquid-crystalline and lamellar to reversed hexagonal phase transitions of aqueous phosphatidylethanolamine dispersions
    • R.N. Lewis, D.A. Mannock, R.N. McElhaney, D.C. Turner, and S.M. Gruner Effect of fatty acyl chain length and structure on the lamellar gel to liquid-crystalline and lamellar to reversed hexagonal phase transitions of aqueous phosphatidylethanolamine dispersions Biochemistry 28 1989 541 548
    • (1989) Biochemistry , vol.28 , pp. 541-548
    • Lewis, R.N.1    Mannock, D.A.2    McElhaney, R.N.3    Turner, D.C.4    Gruner, S.M.5
  • 24
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • H. Luecke, H.T. Richter, and J.K. Lanyi Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution Science 280 1998 1934 1937
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.T.2    Lanyi, J.K.3
  • 25
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 angstroms: Insights into color tuning and transducer interaction
    • H. Luecke, B. Schobert, J.K. Lanyi, E.N. Spudich, and J.L. Spudich Crystal structure of sensory rhodopsin II at 2.4 angstroms: Insights into color tuning and transducer interaction Science 293 2001 1499 1503
    • (2001) Science , vol.293 , pp. 1499-1503
    • Luecke, H.1    Schobert, B.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 26
    • 15444367751 scopus 로고    scopus 로고
    • Strategies and special approaches in growing crystals
    • A. McPherson Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY
    • A. McPherson Strategies and special approaches in growing crystals A. McPherson Crystallization of biological macromolecules 1999 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 271 329
    • (1999) Crystallization of Biological Macromolecules , pp. 271-329
    • McPherson, A.1
  • 27
    • 0242385349 scopus 로고    scopus 로고
    • Detergents destabilize the cubic phase of monoolein: Implications for membrane protein crystallization
    • Y. Misquitta, and M. Caffrey Detergents destabilize the cubic phase of monoolein: Implications for membrane protein crystallization Biophys. J. 85 2003 3084 3096
    • (2003) Biophys. J. , vol.85 , pp. 3084-3096
    • Misquitta, Y.1    Caffrey, M.2
  • 30
    • 0033798841 scopus 로고    scopus 로고
    • Selectivity in lipid binding to the bacterial outer membrane protein ompF
    • A.H. O'Keeffe, M.J. East, and A.G. Lee Selectivity in lipid binding to the bacterial outer membrane protein ompF Biophys. J. 79 2000 2066 2074
    • (2000) Biophys. J. , vol.79 , pp. 2066-2074
    • O'Keeffe, A.H.1    East, M.J.2    Lee, A.G.3
  • 33
    • 11744300646 scopus 로고    scopus 로고
    • Lyotropic and thermotropic phase behavior of hydrated monoacylglycerols: Structure characterization of monovaccenin
    • H. Qiu, and M. Caffrey Lyotropic and thermotropic phase behavior of hydrated monoacylglycerols: Structure characterization of monovaccenin J. Phys. Chem. B 102 1998 4819 4829
    • (1998) J. Phys. Chem. B , vol.102 , pp. 4819-4829
    • Qiu, H.1    Caffrey, M.2
  • 34
    • 0033992338 scopus 로고    scopus 로고
    • Phase properties of the monoolein/water system: Metastability and equilibrium aspects
    • H. Qiu, and M. Caffrey Phase properties of the monoolein/water system: Metastability and equilibrium aspects Biomaterials 21 2000 223 234
    • (2000) Biomaterials , vol.21 , pp. 223-234
    • Qiu, H.1    Caffrey, M.2
  • 35
    • 0035797933 scopus 로고    scopus 로고
    • Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles
    • L.E. Townsley, W.A. Tucker, S. Sham, and J.F. Hinton Structures of gramicidins A, B, and C incorporated into sodium dodecyl sulfate micelles Biochemistry 40 2001 11676 11686
    • (2001) Biochemistry , vol.40 , pp. 11676-11686
    • Townsley, L.E.1    Tucker, W.A.2    Sham, S.3    Hinton, J.F.4
  • 36
    • 0016776797 scopus 로고
    • Simultaneous fluorescence and conductance studies of planar bilayer membranes containing a highly active and fluorescent analog of gramicidin a
    • W.R. Veatch, R. Mathies, M. Eisenberg, and L. Stryer 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    Eisenberg, M.3    Stryer, L.4
  • 37
    • 0031830332 scopus 로고    scopus 로고
    • Recent advances in the high resolution structures of bacterial channels: Gramicidin a
    • B.A. Wallace Recent advances in the high resolution structures of bacterial channels: Gramicidin A J. Struct. Biol. 121 1998 123 141
    • (1998) J. Struct. Biol. , vol.121 , pp. 123-141
    • Wallace, B.A.1
  • 38
    • 0019852927 scopus 로고
    • Conformation of gramicidin a in phospholipid vesicles: Circular dichroism studies of effects of ion binding, chemical modification, and lipid structure
    • B.A. Wallace, W.R. Veatch, and E.R. Blout 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
  • 39
    • 0025819980 scopus 로고
    • Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analog of dioleoylphosphatidylcholine
    • M.C. Wiener, and S.H. White Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analog of dioleoylphosphatidylcholine Biochemistry 30 1991 6997 7008
    • (1991) Biochemistry , vol.30 , pp. 6997-7008
    • Wiener, M.C.1    White, S.H.2
  • 40
    • 0027181230 scopus 로고
    • Thermodynamic, thermomechanical and structural properties of a hydrated asymmetric phosphatidylcholine
    • T. Zhu, and M. Caffrey Thermodynamic, thermomechanical and structural properties of a hydrated asymmetric phosphatidylcholine Biophys. J. 65 1993 939 954
    • (1993) Biophys. J. , vol.65 , pp. 939-954
    • Zhu, T.1    Caffrey, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.