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Volumn 2, Issue 6, 1997, Pages

Folding α-helical membrane proteins: Kinetic studies on bacteriorhodopsin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; MEMBRANE PROTEIN;

EID: 0031302710     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1359-0278(97)00045-x     Document Type: Article
Times cited : (36)

References (46)
  • 1
    • 0020490831 scopus 로고
    • Denaturation and renaturation of bacteriorhodopsin in detergents and lipid-detergent mixtures
    • London, E. & Khorana, H.G. (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
  • 2
    • 0019887931 scopus 로고
    • Refolding of an integral membrane protein. Denaturation, renaturation and reconstitution of intact bacteriorhodopsin and two proteolytic fragments
    • Huang, K.-S., Bayley, H., Liao, M.-J., London, E. & Khorana, H.G. (1981). Refolding of an integral membrane protein. Denaturation, renaturation and reconstitution of intact bacteriorhodopsin and two proteolytic fragments. J. Biol. Chem. 256, 3802-3809.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3802-3809
    • Huang, K.-S.1    Bayley, H.2    Liao, M.-J.3    London, E.4    Khorana, H.G.5
  • 3
    • 0025292355 scopus 로고
    • Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy
    • Henderson, R., Baldwin, J.M., Ceska, T.A., Zemlin, F., Beckmann, E. & Downing, K.H. (1990). Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J. Mol. Biol. 213, 899-929.
    • (1990) J. Mol. Biol. , vol.213 , pp. 899-929
    • Henderson, R.1    Baldwin, J.M.2    Ceska, T.A.3    Zemlin, F.4    Beckmann, E.5    Downing, K.H.6
  • 5
    • 0025898707 scopus 로고
    • Three-dimensional structure of plant light-harvesting complex determined by electron crystallography
    • Kühlbrandt, W. & Wang, D.N. (1991 ). Three-dimensional structure of plant light-harvesting complex determined by electron crystallography. Nature 350, 130-134.
    • (1991) Nature , vol.350 , pp. 130-134
    • Kühlbrandt, W.1    Wang, D.N.2
  • 6
    • 0000683917 scopus 로고
    • Reconstitution of chlorophyll a/b light-harvesting complexes: Xanthophyll-dependent assembly and energy transfer
    • Plumley, F.G. & Schmidt, G.W. (1987). Reconstitution of chlorophyll a/b light-harvesting complexes: xanthophyll-dependent assembly and energy transfer. Proc. Natl Acad Sci. USA 84, 146-150.
    • (1987) Proc. Natl Acad Sci. USA , vol.84 , pp. 146-150
    • Plumley, F.G.1    Schmidt, G.W.2
  • 7
    • 0001456147 scopus 로고
    • Reconsititution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in Escherichia coli
    • Paulsen, H., Rümler, U. & Rüdiger, W. (1990). Reconsititution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in Escherichia coli. Planta 181, 204-211.
    • (1990) Planta , vol.181 , pp. 204-211
    • Paulsen, H.1    Rümler, U.2    Rüdiger, W.3
  • 8
    • 0030000359 scopus 로고    scopus 로고
    • Assembly of the light harvesting chlorophyll a/b complex in vitro. Time-resolved fluorescence measurements
    • Booth, P.J. & Paulsen, H. (1996). Assembly of the light harvesting chlorophyll a/b complex in vitro. Time-resolved fluorescence measurements. Biochemistry 35, 5103-5108.
    • (1996) Biochemistry , vol.35 , pp. 5103-5108
    • Booth, P.J.1    Paulsen, H.2
  • 9
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss, M.S., Abele, U., Weckesser, J., Weite, W., Schiltz, E. & Schulz, G.E. (1991). Molecular architecture and electrostatic properties of a bacterial porin. Science 254, 1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Weite, W.4    Schiltz, E.5    Schulz, G.E.6
  • 10
    • 0026779245 scopus 로고
    • Crystal structures explain functional properties of two E coli porins
    • Cowan, S.W., et al., & Rosenbusch, J.P. (1992). Crystal structures explain functional properties of two E coli porins. Nature 358, 727-733.
    • (1992) Nature , vol.358 , pp. 727-733
    • Cowan, S.W.1    Rosenbusch, J.P.2
  • 11
    • 0025292246 scopus 로고
    • In vitro folding and oligomerization of a membrane protein
    • Eisele, J.-L & Rosenbusch, J.P. (1990). In vitro folding and oligomerization of a membrane protein. J. Biol. Chem. 265, 10217-10220.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10217-10220
    • Eisele, J.-L.1    Rosenbusch, J.P.2
  • 12
    • 0028785347 scopus 로고
    • Kinetics of folding and membrane insertion of a β-barrel membrane protein
    • Surrey, T. & Jähnig, F. (1995). Kinetics of folding and membrane insertion of a β-barrel membrane protein. J. Biol. Chem. 270, 28199-28203.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28199-28203
    • Surrey, T.1    Jähnig, F.2
  • 13
  • 14
    • 0023583873 scopus 로고
    • Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process
    • Popot, J.-L, Gerchman, S.-E. & Engelman, D.M. (1987). Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process. J. Mol. Biol. 198, 655-676.
    • (1987) J. Mol. Biol. , vol.198 , pp. 655-676
    • Popot, J.-L.1    Gerchman, S.-E.2    Engelman, D.M.3
  • 15
    • 0024278712 scopus 로고
    • Bacteriorhodopsin, a membrane protein that uses light to translocate protons
    • Khorana, H.G. (1988). Bacteriorhodopsin, a membrane protein that uses light to translocate protons. J. Biol. Chem. 263, 7439-7442.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7439-7442
    • Khorana, H.G.1
  • 16
    • 0021112513 scopus 로고
    • Regeneration of the native bacteriorhodopsin structure from two chymotryptic fragments
    • Liao, M.-J., London, E. & Khorana, H.G. (1983). Regeneration of the native bacteriorhodopsin structure from two chymotryptic fragments. J. Biol. Chem. 258, 9949-9955.
    • (1983) J. Biol. Chem. , vol.258 , pp. 9949-9955
    • Liao, M.-J.1    London, E.2    Khorana, H.G.3
  • 17
    • 0026642866 scopus 로고
    • Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment
    • Kahn, T.W. & Engelman, D.M. (1992). Bacteriorhodopsin can be refolded from two independently stable transmembrane helices and the complementary five-helix fragment. Biochemistry 31, 6144-6151.
    • (1992) Biochemistry , vol.31 , pp. 6144-6151
    • Kahn, T.W.1    Engelman, D.M.2
  • 18
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two stage model
    • Popot, J.-L. & Engelman, D.M. (1990). Membrane protein folding and oligomerization: the two stage model. Biochemistry 29, 4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.-L.1    Engelman, D.M.2
  • 19
    • 0028138240 scopus 로고
    • Structure and function in rhodopsin. Requirements of a specific structure for the intradiscal domain
    • Anukanth, A. & Khorana, H.G. (1994). Structure and function in rhodopsin. Requirements of a specific structure for the intradiscal domain. J. Biol. Chem. 269, 19738-19744.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19738-19744
    • Anukanth, A.1    Khorana, H.G.2
  • 20
    • 0031012140 scopus 로고    scopus 로고
    • Slow a helical formation during folding of a membrane protein
    • Riley, M.L, Wallace, B.A., Flitsch, S.L. & Booth, P.J. (1997). Slow a helical formation during folding of a membrane protein. Biochemistry 36, 192-196.
    • (1997) Biochemistry , vol.36 , pp. 192-196
    • Riley, M.L.1    Wallace, B.A.2    Flitsch, S.L.3    Booth, P.J.4
  • 21
    • 0030904764 scopus 로고    scopus 로고
    • Transient intermediates in the regeneration of bacteriorhodopsin investigated by time-resolved absorption spectroscopy
    • Booth, PJ. & Farooq, A. (1997). Transient intermediates in the regeneration of bacteriorhodopsin investigated by time-resolved absorption spectroscopy. Eur. J. Biochem. 246, 674-680.
    • (1997) Eur. J. Biochem. , vol.246 , pp. 674-680
    • Booth, P.J.1    Farooq, A.2
  • 22
    • 0026770209 scopus 로고
    • Refolding and oriented insertion of a membrane protein into a lipid bilayer
    • Surrey, T. & Jähnig, F. (1992). Refolding and oriented insertion of a membrane protein into a lipid bilayer. Proc. Natl Acad. Sci. USA 89, 7457-7461.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7457-7461
    • Surrey, T.1    Jähnig, F.2
  • 23
    • 0027233533 scopus 로고
    • Refolding and proton-pumping activity of a polyethylene-glycol bacteriorhodopsin water-soluble conjugate
    • Sirokman, G. & Fasman, G.D. (1993). Refolding and proton-pumping activity of a polyethylene-glycol bacteriorhodopsin water-soluble conjugate. Protein Sci. 2, 1161-1170.
    • (1993) Protein Sci. , vol.2 , pp. 1161-1170
    • Sirokman, G.1    Fasman, G.D.2
  • 24
    • 0029061507 scopus 로고
    • A polyethylene glycol water-soluble conjugate of porin: Refolding to the native state
    • Wei, J. & Fasman, G.D. (1995). A polyethylene glycol) water-soluble conjugate of porin: refolding to the native state. Biochemistry 34, 6408-6415.
    • (1995) Biochemistry , vol.34 , pp. 6408-6415
    • Wei, J.1    Fasman, G.D.2
  • 25
    • 0029943869 scopus 로고    scopus 로고
    • Retinal binding during folding and assembly of the membrane protein bacteriorhodopsin
    • Booth, P.J., Farooq, A. & Flitsch, S.L. (1996). Retinal binding during folding and assembly of the membrane protein bacteriorhodopsin. Biochemistry 35, 5902-5909.
    • (1996) Biochemistry , vol.35 , pp. 5902-5909
    • Booth, P.J.1    Farooq, A.2    Flitsch, S.L.3
  • 26
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima, K. (1989). The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6, 87-103.
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 27
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews, C.R. (1993). Pathways of protein folding. Annu. Rev. Biochem. 62, 653-683.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 28
    • 0031055942 scopus 로고    scopus 로고
    • Kinetic role of early intermediates in protein folding
    • Roder, H. & Colon, W. (1997). Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 15-28
    • Roder, H.1    Colon, W.2
  • 30
    • 0031021150 scopus 로고    scopus 로고
    • Evidence that bilayer bending rigidity affects membrane protein folding
    • Booth, P.J., et al., & Wright, P. (1997). Evidence that bilayer bending rigidity affects membrane protein folding. Biochemistry 36, 197-203.
    • (1997) Biochemistry , vol.36 , pp. 197-203
    • Booth, P.J.1    Wright, P.2
  • 31
    • 0021755639 scopus 로고
    • Differential light scattering and absorption flattening. Optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles
    • Mao, D. & Wallace, B.A. (1984). Differential light scattering and absorption flattening. Optical effects are minimal in the circular dichroism spectra of small unilamellar vesicles. Biochemistry 23, 2667-2673.
    • (1984) Biochemistry , vol.23 , pp. 2667-2673
    • Mao, D.1    Wallace, B.A.2
  • 32
    • 0001913674 scopus 로고
    • Folding and assembly of integral membrane proteins: An introduction
    • S.H. White, ed., Oxford University Press, New York.
    • Popot, J.-L, de Vitry, C. & Atteia, A. (1994). Folding and assembly of integral membrane proteins: an introduction. In Membrane Protein Structure. (S.H. White, ed.), pp. 41-96, Oxford University Press, New York.
    • (1994) In Membrane Protein Structure. , pp. 41-96
    • Popot, J.-L.1    De Vitry, C.2    Atteia, A.3
  • 33
    • 0016711868 scopus 로고
    • Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues
    • Brandts, J.F., Halvorson, H.R. & Brennan, M. (1975). Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14, 4953-4963.
    • (1975) Biochemistry , vol.14 , pp. 4953-4963
    • Brandts, J.F.1    Halvorson, H.R.2    Brennan, M.3
  • 34
    • 0001849773 scopus 로고
    • Proline isomerization as a rate-limiting step
    • B.D. Harnes Oxford University Press, New York.
    • Nall, B.T. (1994). Proline isomerization as a rate-limiting step. In Mechanisms of Protein Folding. (B.D. Harnes & D.M. Glover, eds), pp. 80-103, Oxford University Press, New York.
    • (1994) Mechanisms of Protein Folding , pp. 80-103
    • Nall, B.T.1
  • 35
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for nonbilayer lipids
    • Gruner, S.M. (1985). Intrinsic curvature hypothesis for biomembrane lipid composition: a role for nonbilayer lipids. Proc. Natl Acad. Sci. USA 82, 3665-3669.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 36
    • 0025993884 scopus 로고    scopus 로고
    • Physical-properties of the fluid lipid-bilayer component of cell membranes: A perspective
    • Bloom, M., Evans, E. & Mouritsen, O.G. (1997). Physical-properties of the fluid lipid-bilayer component of cell membranes: a perspective. Quart. Rev. Biophys. 24, 293-397.
    • (1997) Quart. Rev. Biophys. , vol.24 , pp. 293-397
    • Bloom, M.1    Evans, E.2    Mouritsen, O.G.3
  • 37
    • 0025134135 scopus 로고
    • Structure of the inverted hexagonal (Hll) phase, and non-lammellar phase transitions of lipids
    • Seddon, J.M. (1990). Structure of the inverted hexagonal (Hll) phase, and non-lammellar phase transitions of lipids. Biochim. Biophys. Acta 1031, 1-69.
    • (1990) Biochim. Biophys. Acta , vol.1031 , pp. 1-69
    • Seddon, J.M.1
  • 39
    • 0030606012 scopus 로고    scopus 로고
    • Lateral pressure in membranes
    • Marsh, D. (1996). Lateral pressure in membranes. Biochim. Biophys. Acta 1286, 183-223.
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 183-223
    • Marsh, D.1
  • 40
    • 0028140457 scopus 로고
    • Measuring the elastic parameters for inverse bicontinuous cubic phases
    • Templer, R.H., Seddon, J.M. & Warrender, N.A. (1994). Measuring the elastic parameters for inverse bicontinuous cubic phases. Biophys. Chem. 49, 1-12.
    • (1994) Biophys. Chem. , vol.49 , pp. 1-12
    • Templer, R.H.1    Seddon, J.M.2    Warrender, N.A.3
  • 41
    • 0029992660 scopus 로고    scopus 로고
    • Lipidic cubic phases: A novel concept for the crystallization of membrane proteins
    • Landau, E.M. & Rosenbusch, J.P. (1996). Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc. Natl Acad. Sci. USA 93, 14532-14535.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 14532-14535
    • Landau, E.M.1    Rosenbusch, J.P.2
  • 42
    • 0028086531 scopus 로고
    • Specificity and promiscuity in membrane helix interactions
    • Lemmon, M.A. & Engelman, D.M. (1994). Specificity and promiscuity in membrane helix interactions. Quart. Rev. Biophys. 27, 157-218.
    • (1994) Quart. Rev. Biophys. , vol.27 , pp. 157-218
    • Lemmon, M.A.1    Engelman, D.M.2
  • 43
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix dimer: Structure and implications
    • MacKenzie, K.R., Prestegard, J.H. & Engelman, D.M. (1997). A transmembrane helix dimer: structure and implications. Science 276, 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 44
    • 0017377436 scopus 로고
    • Studies on the retinal-protein interaction in bacteriorhodopsin
    • Schreckenbach, T., Walckhoff, B. & Oesterhelt, D. (1977). Studies on the retinal-protein interaction in bacteriorhodopsin. Eur. J. Biochem. 76, 499-511.
    • (1977) Eur. J. Biochem. , vol.76 , pp. 499-511
    • Schreckenbach, T.1    Walckhoff, B.2    Oesterhelt, D.3
  • 45
    • 0026686623 scopus 로고
    • Thermodynamic measurements of the contributions of helixconnecting loops and of retinal to the stability of bacteriorhodopsin
    • Kahn, T.W., Sturtevant, J.M. & Engelman, D.M. (1992). Thermodynamic measurements of the contributions of helixconnecting loops and of retinal to the stability of bacteriorhodopsin. Biochemistry 31, 8829-8839.
    • (1992) Biochemistry , vol.31 , pp. 8829-8839
    • Kahn, T.W.1    Sturtevant, J.M.2    Engelman, D.M.3
  • 46
    • 0027301940 scopus 로고
    • Pigments induce folding of light-harvesting chlorophyll a/b-binding protein
    • Paulsen, H., Finkenzeller, B. & Kühlein, N. (1993). Pigments induce folding of light-harvesting chlorophyll a/b-binding protein. Eur. J. Biochem. 215, 809-817.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 809-817
    • Paulsen, H.1    Finkenzeller, B.2    Kühlein, N.3


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