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Volumn 94, Issue 9, 2008, Pages 3523-3537

Bacteriorhodopsin/Amphipol complexes: Structural and functional properties

Author keywords

[No Author keywords available]

Indexed keywords

AMPHIPOL A8 35; AMPHIPOL A8-35; BACTERIAL PROTEIN; BACTERIORHODOPSIN; LIPID; N OCTYL BETA D THIOGLUCOPYRANOSIDE; N-OCTYL-BETA-D-THIOGLUCOPYRANOSIDE; POLYMER; PROPYLAMINE; THIOGLYCOSIDE;

EID: 43649083325     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.121848     Document Type: Article
Times cited : (79)

References (54)
  • 1
    • 85031367321 scopus 로고    scopus 로고
    • http://blanco.biomol.uci.edu/Membrane-Proteins-xtal.html.
  • 2
    • 85031364527 scopus 로고    scopus 로고
    • http://www.mpibp-frankfurt.mpg.de/michel/public/memprotstruct.html.
  • 3
    • 0030451437 scopus 로고    scopus 로고
    • Amphipols: Polymers that keep membrane proteins soluble in aqueous solutions
    • Tribet, C., R. Audebert, and J.-L. Popot. 1996. Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. Proc. Natl. Acad. Sci. USA. 93:15047-15050.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15047-15050
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 6
    • 35148874303 scopus 로고    scopus 로고
    • Dynamics of membrane protein/amphipol association studied by Forster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins
    • Zoonens, M., F. Giusti, F. Zito, and J.-L. Popot. 2007. Dynamics of membrane protein/amphipol association studied by Forster resonance energy transfer. Implications for in vitro studies of amphipol-stabilized membrane proteins. Biochemistry. 46:10392-10404.
    • (2007) Biochemistry , vol.46 , pp. 10392-10404
    • Zoonens, M.1    Giusti, F.2    Zito, F.3    Popot, J.-L.4
  • 8
  • 9
    • 34548329761 scopus 로고    scopus 로고
    • The use of amphipathic polymers for cryo-electron microscopy of NADH:ubiquinone oxidoreductase (complex I)
    • Flotenmeyer, M., H. Weiss, C. Tribet, J.-L. Popot, and K. Leonard. 2007. The use of amphipathic polymers for cryo-electron microscopy of NADH:ubiquinone oxidoreductase (complex I). J. Microsc. 227: 229-235.
    • (2007) J. Microsc , vol.227 , pp. 229-235
    • Flotenmeyer, M.1    Weiss, H.2    Tribet, C.3    Popot, J.-L.4    Leonard, K.5
  • 10
    • 0033567092 scopus 로고    scopus 로고
    • Protein, lipid and water organization in bacteriorhodopsin crystals: A molecular view of the purple membrane at 1.9 Å resolution
    • Belrhali, H., P. Nollert, A. Royant, C. Menzel, J. P. Rosenbusch, E. M. Landau, and E. Pebay-Peyroula. 1999. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 Å resolution. Struct. Fold. Des. 7:909-917.
    • (1999) Struct. Fold. Des , vol.7 , pp. 909-917
    • Belrhali, H.1    Nollert, P.2    Royant, A.3    Menzel, C.4    Rosenbusch, J.P.5    Landau, E.M.6    Pebay-Peyroula, E.7
  • 11
    • 32344431772 scopus 로고    scopus 로고
    • Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35
    • Gohon, Y., F. Giusti, C. Prata, D. Charvolin, P. Timmins, C. Ebel, C. Tribet, and J.-L. Popot. 2006. Well-defined nanoparticles formed by hydrophobic assembly of a short and polydisperse random terpolymer, amphipol A8-35. Langmuir. 22:1281-1290.
    • (2006) Langmuir , vol.22 , pp. 1281-1290
    • Gohon, Y.1    Giusti, F.2    Prata, C.3    Charvolin, D.4    Timmins, P.5    Ebel, C.6    Tribet, C.7    Popot, J.-L.8
  • 13
    • 0016376428 scopus 로고
    • Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane
    • Oesterhelt, D., and W. Stoeckenius. 1974. Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane. Methods Enzymol. 31:667-678.
    • (1974) Methods Enzymol , vol.31 , pp. 667-678
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 14
    • 0344667489 scopus 로고    scopus 로고
    • Osmotic shock induces the presence of glycocardiolipin in the purple membrane of Halobacterium salinarum
    • Lobasso, S., P. Lopalco, V. M. Lattanzio, and A. Corcelli. 2003. Osmotic shock induces the presence of glycocardiolipin in the purple membrane of Halobacterium salinarum. J. Lipid Res. 44:2120-2126.
    • (2003) J. Lipid Res , vol.44 , pp. 2120-2126
    • Lobasso, S.1    Lopalco, P.2    Lattanzio, V.M.3    Corcelli, A.4
  • 15
    • 0020490831 scopus 로고
    • Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures
    • London, E., and H. G. Khorana. 1982. Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures. J. Biol. Chem. 257:7003-7011.
    • (1982) J. Biol. Chem , vol.257 , pp. 7003-7011
    • London, E.1    Khorana, H.G.2
  • 17
    • 0032480785 scopus 로고    scopus 로고
    • Electrostatic interactions at the donor side of the photosynthetic reaction center of Rhodopseudomonas viridis
    • Baymann, F., and F. Rappaport. 1998. Electrostatic interactions at the donor side of the photosynthetic reaction center of Rhodopseudomonas viridis. Biochemistry. 37:15320-15326.
    • (1998) Biochemistry , vol.37 , pp. 15320-15326
    • Baymann, F.1    Rappaport, F.2
  • 19
    • 0028890265 scopus 로고
    • Calibration of size-exclusion chromatography: Use of a double Gaussian distribution function to describe pore sizes
    • Harlan, J. E., D. Picot, P. J. Loll, and R. M. Garavito. 1995. Calibration of size-exclusion chromatography: use of a double Gaussian distribution function to describe pore sizes. Anal. Biochem. 224:557-563.
    • (1995) Anal. Biochem , vol.224 , pp. 557-563
    • Harlan, J.E.1    Picot, D.2    Loll, P.J.3    Garavito, R.M.4
  • 20
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. 37:911-917.
    • (1959) Can. J. Biochem , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 21
    • 21244499919 scopus 로고
    • Lipids of purple membranes from extreme halophiles and of methanogenic bacteria
    • Kates, M., S. D. Kushawa, and G. D. Sprott. 1982. Lipids of purple membranes from extreme halophiles and of methanogenic bacteria. Methods Enzymol. 88:98-111.
    • (1982) Methods Enzymol , vol.88 , pp. 98-111
    • Kates, M.1    Kushawa, S.D.2    Sprott, G.D.3
  • 22
    • 0014779155 scopus 로고
    • Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser, G., S. Fleischer, and A. Yamamoto. 1970. Two-dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids. 5:494-496.
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fleischer, S.2    Yamamoto, A.3
  • 23
    • 38149020669 scopus 로고    scopus 로고
    • Analytical ultracentrifugation. State of the art and perspectives
    • V. Uversky and E. A. Permyakov, editors. Nova Science, New York
    • Ebel, C. 2007. Analytical ultracentrifugation. State of the art and perspectives. In Protein Structures: Methods in Protein Structure and Stability Analysis. V. Uversky and E. A. Permyakov, editors. Nova Science, New York. 229-260.
    • (2007) Protein Structures: Methods in Protein Structure and Stability Analysis , pp. 229-260
    • Ebel, C.1
  • 24
    • 85031356844 scopus 로고    scopus 로고
    • www.analyticalultracentrifugation.com.
  • 25
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78:1606-1619.
    • (2000) Biophys. J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 26
    • 85031367986 scopus 로고    scopus 로고
    • http://leonardo.fcu.um.es/macromol/programs/hydro++/hydro++.htm.
  • 27
    • 0019562446 scopus 로고
    • Forward scattering of light, X-rays and neutrons
    • Eisenberg, H. 1981. Forward scattering of light, X-rays and neutrons. Q. Rev. Biophys. 14:141-172.
    • (1981) Q. Rev. Biophys , vol.14 , pp. 141-172
    • Eisenberg, H.1
  • 30
    • 1642375072 scopus 로고
    • Micelle shape and size
    • Tanford, C. 1972. Micelle shape and size. J. Phys. Chem. 76:3020-3024.
    • (1972) J. Phys. Chem , vol.76 , pp. 3020-3024
    • Tanford, C.1
  • 31
    • 85031367357 scopus 로고    scopus 로고
    • Merck Index
    • Maryadele J. O'Neil, editor, 13th ed, Merck Publishing, Whitehouse Station, N.J
    • Maryadele J. O'Neil, editor. 2001. Merck Index, 13th ed. Monograph No. 4497. Merck Publishing, Whitehouse Station, N.J. 799.
    • (2001) Monograph , vol.4497 , pp. 799
  • 32
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins, S. J. 1986. Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157:169-180.
    • (1986) Eur. J. Biochem , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 33
    • 84978555349 scopus 로고
    • Interpretation of small-angle scattering functions of dilute solutions and gases. A representation of the structures related to a one-particle scattering function
    • Stuhrmann, H. B. 1970. Interpretation of small-angle scattering functions of dilute solutions and gases. A representation of the structures related to a one-particle scattering function. Acta Crystallogr. A. 26: 297-306.
    • (1970) Acta Crystallogr. A , vol.26 , pp. 297-306
    • Stuhrmann, H.B.1
  • 34
    • 11144318547 scopus 로고
    • Contrast variation of the small-angle neutron scattering of globular particles: The influence of hydrogen exchange
    • Witz, J. 1983. Contrast variation of the small-angle neutron scattering of globular particles: the influence of hydrogen exchange. Acta Crystallogr. A. 39:706-711.
    • (1983) Acta Crystallogr. A , vol.39 , pp. 706-711
    • Witz, J.1
  • 35
    • 0027995683 scopus 로고    scopus 로고
    • Kleywegt,G.J.,andT.A.Jones.1994.Detection,delineation,measurement and display of cavities in macromolecular structures. Acta Crystallogr. D Biol. Crystallogr. 50:178-185.
    • Kleywegt,G.J.,andT.A.Jones.1994.Detection,delineation,measurement and display of cavities in macromolecular structures. Acta Crystallogr. D Biol. Crystallogr. 50:178-185.
  • 36
    • 85031363718 scopus 로고    scopus 로고
    • http://www.embl-hamburg.de/ExternalInfo/Research/Sax/cryson.html.
  • 38
    • 0025731582 scopus 로고
    • Effects of detergent environments on the photocycle of purified monomelic bacteriorhodopsin
    • Milder, S. J., T. E. Thorgeirsson, L. J. Miercke, R. M. Stroud, and D. S. Kliger. 1991. Effects of detergent environments on the photocycle of purified monomelic bacteriorhodopsin. Biochemistry. 30:1751-1761.
    • (1991) Biochemistry , vol.30 , pp. 1751-1761
    • Milder, S.J.1    Thorgeirsson, T.E.2    Miercke, L.J.3    Stroud, R.M.4    Kliger, D.S.5
  • 39
    • 0018135255 scopus 로고
    • Formation and properties of bacteriorhodopsin monomers in the non-ionic detergents octyl-β-D-glucoside and Triton X-100
    • Dencher, N. A., and M. P. Heyn. 1978. Formation and properties of bacteriorhodopsin monomers in the non-ionic detergents octyl-β-D-glucoside and Triton X-100. FEBS Lett. 96:322-326.
    • (1978) FEBS Lett , vol.96 , pp. 322-326
    • Dencher, N.A.1    Heyn, M.P.2
  • 40
    • 0025895761 scopus 로고
    • Detergent delipidation and solubilization strategies for high-resolution NMR of the membrane protein bacteriorhodopsin
    • Seigneuret, M., J.-M. Neumann, and J.-L. Rigaud. 1991. Detergent delipidation and solubilization strategies for high-resolution NMR of the membrane protein bacteriorhodopsin. J. Biol. Chem. 266:10066-10069.
    • (1991) J. Biol. Chem , vol.266 , pp. 10066-10069
    • Seigneuret, M.1    Neumann, J.-M.2    Rigaud, J.-L.3
  • 42
    • 0034658269 scopus 로고    scopus 로고
    • Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography
    • Vonck, J. 2000. Structure of the bacteriorhodopsin mutant F219L N intermediate revealed by electron crystallography. EMBO J. 19:2152-2160.
    • (2000) EMBO J , vol.19 , pp. 2152-2160
    • Vonck, J.1
  • 43
    • 0037174145 scopus 로고    scopus 로고
    • Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: Molecular interactions vs. physical constraints
    • Martinez, K. L., Y. Gohon, P.-J. Corringer, C. Tribet, F. Mérola, J.-P. Changeux, and J.-L. Popot. 2002. Allosteric transitions of Torpedo acetylcholine receptor in lipids, detergent and amphipols: molecular interactions vs. physical constraints. FEBS Lett. 528:251-256.
    • (2002) FEBS Lett , vol.528 , pp. 251-256
    • Martinez, K.L.1    Gohon, Y.2    Corringer, P.-J.3    Tribet, C.4    Mérola, F.5    Changeux, J.-P.6    Popot, J.-L.7
  • 45
    • 0037043709 scopus 로고    scopus 로고
    • Structural changes in the calcium pump accompanying the dissociation of calcium
    • Toyoshima, C., and H. Nomura. 2002. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature. 418: 605-611.
    • (2002) Nature , vol.418 , pp. 605-611
    • Toyoshima, C.1    Nomura, H.2
  • 46
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa, A., Y. Fujiyoshi, and N. Unwin. 2003. Structure and gating mechanism of the acetylcholine receptor pore. Nature. 423:949-955.
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 47
    • 0242488935 scopus 로고    scopus 로고
    • Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy
    • Unwin, N. 2003. Structure and action of the nicotinic acetylcholine receptor explored by electron microscopy. FEBS Lett. 555:91-95.
    • (2003) FEBS Lett , vol.555 , pp. 91-95
    • Unwin, N.1
  • 48
    • 0031249290 scopus 로고    scopus 로고
    • Stabilisation of hydro- phobic colloidal dispersions in water with amphiphilic polymers: Application to integral membrane proteins
    • Tribet, C., R. Audebert, and J.-L. Popot. 1997. Stabilisation of hydro- phobic colloidal dispersions in water with amphiphilic polymers: application to integral membrane proteins. Langmuir. 13:5570-5576.
    • (1997) Langmuir , vol.13 , pp. 5570-5576
    • Tribet, C.1    Audebert, R.2    Popot, J.-L.3
  • 51
    • 0027283560 scopus 로고
    • Detergent binding as a measure of hydrophobic surface area of integral membrane proteins
    • Møller, J. V., and M. le Maire. 1993. Detergent binding as a measure of hydrophobic surface area of integral membrane proteins. J. Biol. Chem. 268:18659-18672.
    • (1993) J. Biol. Chem , vol.268 , pp. 18659-18672
    • Møller, J.V.1    le Maire, M.2
  • 52
    • 36048943576 scopus 로고    scopus 로고
    • Complexation of integral membrane proteins by phosphorylcholine- based amphipols
    • Diab, C., C. Tribet, Y. Gohon, J.-L. Popot, and F. M. Winnik. 2007. Complexation of integral membrane proteins by phosphorylcholine- based amphipols. Biochim. Biophys. Acta. 1768:2737-2747.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 2737-2747
    • Diab, C.1    Tribet, C.2    Gohon, Y.3    Popot, J.-L.4    Winnik, F.M.5
  • 54
    • 0342484454 scopus 로고    scopus 로고
    • Analogies between halorhodopsin and bacteriorhodopsin
    • Váró, G. 2000. Analogies between halorhodopsin and bacteriorhodopsin. Biochim. Biophys. Acta. 1460:220-229.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 220-229
    • Váró, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.