메뉴 건너뛰기




Volumn 273, Issue 5, 1997, Pages 1004-1019

Assessment of the aggregation state of integral membrane proteins in reconstituted phospholipid vesicles using small angle neutron scattering

Author keywords

Aggregation state; Bacteriorhodopsin; Membrane proteins; Phospholipid vesicles; Small angle neutron scattering

Indexed keywords

BACTERIORHODOPSIN; MEMBRANE PROTEIN;

EID: 0031567785     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1330     Document Type: Article
Times cited : (29)

References (58)
  • 1
    • 0023895718 scopus 로고
    • Temperature-induced phase transitions in proteins and lipids. Volume and heat capacity effects
    • Bendzko, P. I., Pfeil, W. A., Privalov, P. L. & Tiktopulo, E. I. (1988). Temperature-induced phase transitions in proteins and lipids. Volume and heat capacity effects. Biophys. Chem. 29, 301-307.
    • (1988) Biophys. Chem. , vol.29 , pp. 301-307
    • Bendzko, P.I.1    Pfeil, W.A.2    Privalov, P.L.3    Tiktopulo, E.I.4
  • 2
    • 0026694442 scopus 로고
    • Intramembrane helix-helix association in oligomerization and transmembrane signaling
    • Bormann, B. J. & Engelman, D. M. (1992). Intramembrane helix-helix association in oligomerization and transmembrane signaling. Annu. Rev. Biophys. Biomol. Struct. 21, 223-242.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 223-242
    • Bormann, B.J.1    Engelman, D.M.2
  • 3
    • 0017927954 scopus 로고
    • Neutron diffraction studies on selectively deuterated phospholipid bilayers
    • Büldt, G., Gally, H. U., Seelig, A., Seelig, J. & Zaccaï, G. (1978). Neutron diffraction studies on selectively deuterated phospholipid bilayers. Nature, 271, 182-184.
    • (1978) Nature , vol.271 , pp. 182-184
    • Büldt, G.1    Gally, H.U.2    Seelig, A.3    Seelig, J.4    Zaccaï, G.5
  • 4
    • 0018792901 scopus 로고
    • Neutron diffraction studies on phosphatidylcholine model membranes. I. Head group conformation
    • Büldt, G., Gally, H. U., Seelig, J. & Zaccaï, G. (1979). Neutron diffraction studies on phosphatidylcholine model membranes. I. Head group conformation. J. Mol. Biol. 134, 673-691.
    • (1979) J. Mol. Biol. , vol.134 , pp. 673-691
    • Büldt, G.1    Gally, H.U.2    Seelig, J.3    Zaccaï, G.4
  • 6
    • 0025912307 scopus 로고
    • Comparison of epidermal growth factor (EGF) receptor-receptor interactions in intact A431 cells and isolated plasma membranes. Large scale receptor micro-aggregation is not detected during EGF-stimulated early events
    • Carraway, K. L. & Cerione, R. A. (1991). Comparison of epidermal growth factor (EGF) receptor-receptor interactions in intact A431 cells and isolated plasma membranes. Large scale receptor micro-aggregation is not detected during EGF-stimulated early events. J. Biol. Chem. 266, 8899-8906.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8899-8906
    • Carraway, K.L.1    Cerione, R.A.2
  • 7
    • 0024309393 scopus 로고
    • Visualization of epidermal growth factor (EGF) receptor aggregation in plasma membranes by fluorescence resonance energy transfer. Correlation of receptor activation with aggregation
    • Carraway, K. L., Koland, J. G. & Cerione, R. A. (1989). Visualization of epidermal growth factor (EGF) receptor aggregation in plasma membranes by fluorescence resonance energy transfer. Correlation of receptor activation with aggregation. J. Biol. Chem. 264, 8699-8707.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8699-8707
    • Carraway, K.L.1    Koland, J.G.2    Cerione, R.A.3
  • 8
    • 0025938224 scopus 로고
    • Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity
    • Casey, J. R. & Reithmeier, R. A. (1991). Analysis of the oligomeric state of Band 3, the anion transport protein of the human erythrocyte membrane, by size exclusion high performance liquid chromatography. Oligomeric stability and origin of heterogeneity. J. Biol. Chem. 266, 15726-15737.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15726-15737
    • Casey, J.R.1    Reithmeier, R.A.2
  • 9
    • 0017819030 scopus 로고
    • Temperature-dependent aggregation of bacteriorhodopsin in dipalmitoyl and dimyristoylphosphatidylcholine vesicles
    • Cherry, R. J., Moøller, U., Henderson, R. & Heyn, M. P. (1978). Temperature-dependent aggregation of bacteriorhodopsin in dipalmitoyl and dimyristoylphosphatidylcholine vesicles. J. Mol. Biol. 121, 283-298.
    • (1978) J. Mol. Biol. , vol.121 , pp. 283-298
    • Cherry, R.J.1    Moøller, U.2    Henderson, R.3    Heyn, M.P.4
  • 10
    • 0023848318 scopus 로고
    • Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent
    • Cochet, C., Kashles, O., Chambaz, E. M., Borrello, I., King, C. R. & Schlessinger, J. (1988). Demonstration of epidermal growth factor-induced receptor dimerization in living cells using a chemical covalent cross-linking agent. J. Biol. Chem. 263, 3290-3295.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3290-3295
    • Cochet, C.1    Kashles, O.2    Chambaz, E.M.3    Borrello, I.4    King, C.R.5    Schlessinger, J.6
  • 11
    • 0023738047 scopus 로고
    • Comparison of the structure of myosin subfragment 1 bound to actin and free in solution. A neutron scattering study using actin made "invisible" by deuteration
    • Curmi, P. M., Stone, D. B., Schneider, D. K., Spudich, J. A. & Mendelson, R. A. (1988). Comparison of the structure of myosin subfragment 1 bound to actin and free in solution. A neutron scattering study using actin made "invisible" by deuteration. J. Mol. Biol. 203, 781-798.
    • (1988) J. Mol. Biol. , vol.203 , pp. 781-798
    • Curmi, P.M.1    Stone, D.B.2    Schneider, D.K.3    Spudich, J.A.4    Mendelson, R.A.5
  • 12
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • de Vos, A. M., Ultsch, M. & Kossiakoff, A. A. (1992). Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science, 255, 306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • De Vos, A.M.1    Ultsch, M.2    Kossiakoff, A.A.3
  • 13
    • 0025608693 scopus 로고
    • Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange
    • Earnest, T. N., Herzfeld, J. & Rothschild, K. J. (1990). Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchange. Biophys. J. 58, 1539-1546.
    • (1990) Biophys. J. , vol.58 , pp. 1539-1546
    • Earnest, T.N.1    Herzfeld, J.2    Rothschild, K.J.3
  • 16
    • 0022387904 scopus 로고
    • Chemical and biochemical cross-linking of membrane components
    • Gaffney, B. J. (1985). Chemical and biochemical cross-linking of membrane components. Biochim. Biophys. Acta, 822, 289-317.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 289-317
    • Gaffney, B.J.1
  • 20
    • 0029903197 scopus 로고    scopus 로고
    • Electron-crystallographic refinement of the structure of bacteriorhodopsin
    • Grigorieff, N., Ceska, T. A., Downing, K. H., Baldwin, J. M. & Henderson, R. (1996). Electron-crystallographic refinement of the structure of bacteriorhodopsin. J. Mol. Biol. 259, 393-421.
    • (1996) J. Mol. Biol. , vol.259 , pp. 393-421
    • Grigorieff, N.1    Ceska, T.A.2    Downing, K.H.3    Baldwin, J.M.4    Henderson, R.5
  • 23
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin, C. H. (1995). Dimerization of cell surface receptors in signal transduction. Cell, 80, 213-223.
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 24
    • 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
  • 25
    • 0242285207 scopus 로고
    • Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid
    • Huang, K. S., Bayley, H. & Khorana, H. G. (1980). Delipidation of bacteriorhodopsin and reconstitution with exogenous phospholipid. Proc. Natl Acad. Sci. USA, 77, 323-327.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 323-327
    • Huang, K.S.1    Bayley, H.2    Khorana, H.G.3
  • 26
    • 0024461745 scopus 로고
    • Protein oligomerization in the endoplasmic reticulum
    • Hurtley, S. M. & Helenius, A. (1989). Protein oligomerization in the endoplasmic reticulum. Annu. Rev. Cell Biol. 5, 277-307.
    • (1989) Annu. Rev. Cell Biol. , vol.5 , pp. 277-307
    • Hurtley, S.M.1    Helenius, A.2
  • 27
    • 0001277638 scopus 로고
    • The small angle neutron scattering station D11 at the Institut Laue-Langevin
    • Ibel, K. (1976). The small angle neutron scattering station D11 at the Institut Laue-Langevin. J. Appl. Crystallog. 9, 296-309.
    • (1976) J. Appl. Crystallog. , vol.9 , pp. 296-309
    • Ibel, K.1
  • 28
    • 0016640142 scopus 로고
    • Comparison of neutron and X-ray scattering of dilute myoglobin solutions
    • Ibel, K. & Stuhrmann, H. B. (1975). Comparison of neutron and X-ray scattering of dilute myoglobin solutions. J. Mol. Biol. 93, 255-265.
    • (1975) J. Mol. Biol. , vol.93 , pp. 255-265
    • Ibel, K.1    Stuhrmann, H.B.2
  • 29
    • 0001339660 scopus 로고
    • The study of biological structures by neutron scattering from solution
    • Jacrot, B. (1976). The study of biological structures by neutron scattering from solution. Rep. Prog. Phys. 39, 911-953.
    • (1976) Rep. Prog. Phys. , vol.39 , pp. 911-953
    • Jacrot, B.1
  • 30
    • 84985698663 scopus 로고
    • Determination of molecular weight by neutron scattering
    • Jacrot, B. & Zaccaï, G. (1981). Determination of molecular weight by neutron scattering. Biopholymers, 20, 2414-2426.
    • (1981) Biopholymers , vol.20 , pp. 2414-2426
    • Jacrot, B.1    Zaccaï, G.2
  • 31
    • 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
  • 32
    • 0019889788 scopus 로고
    • Small-angle neutron scattering study of lipid phase diagrams by the contrast variation method
    • Knoll, W., Ibel, K. & Sackmann, E. (1981). Small-angle neutron scattering study of lipid phase diagrams by the contrast variation method. Biochemistry, 20, 6379-6383.
    • (1981) Biochemistry , vol.20 , pp. 6379-6383
    • Knoll, W.1    Ibel, K.2    Sackmann, E.3
  • 33
    • 0024485714 scopus 로고
    • Rapid calculation of the solution scattering profile from a macromolecule of known structure
    • Lattman, E. E. (1989). Rapid calculation of the solution scattering profile from a macromolecule of known structure. Proteins: Struct. Funct. Genet. 5, 149-155.
    • (1989) Proteins: Struct. Funct. Genet. , vol.5 , pp. 149-155
    • Lattman, E.E.1
  • 34
    • 0021769831 scopus 로고
    • Neutron small-angle scattering studies of ribonuclease in mixed aqueous solutions and determination of the preferentially bound water
    • Lehmann, N. S. & Zaccaï, G. (1984). Neutron small-angle scattering studies of ribonuclease in mixed aqueous solutions and determination of the preferentially bound water. Biochemistry, 23, 1939-1942.
    • (1984) Biochemistry , vol.23 , pp. 1939-1942
    • Lehmann, N.S.1    Zaccaï, G.2
  • 35
    • 0022458798 scopus 로고
    • Protein-protein interactions in membranes: Concepts and the example of calcium ATPase from the sarcoplasmic reticulum
    • le, Maire M. (1986). Protein-protein interactions in membranes: concepts and the example of calcium ATPase from the sarcoplasmic reticulum. Biochimie, 68, 395-400.
    • (1986) Biochimie , vol.68 , pp. 395-400
    • Le Maire, M.1
  • 36
    • 0022453762 scopus 로고
    • The use of high-performance liquid chromatography for the determination of size and molecular weight of proteins: A caution and a list of membrane proteins suitable as standards
    • le Maire, M., Aggerbeck, L. P., Monteilhet, C., Andersen, J. P. & Møller, J. V. (1986). The use of high-performance liquid chromatography for the determination of size and molecular weight of proteins: a caution and a list of membrane proteins suitable as standards. Anal. Biochem. 154, 525-535.
    • (1986) Anal. Biochem. , vol.154 , pp. 525-535
    • Le Maire, M.1    Aggerbeck, L.P.2    Monteilhet, C.3    Andersen, J.P.4    Møller, J.V.5
  • 37
    • 0025248416 scopus 로고
    • Effects of ionizing radiations on proteins. Evidence of non-random fragmentations and a caution in the use of the method for determination of molecular mass
    • le, Maire M., Thauvette, L., de Foresta, B., Viel, A., Beauregard, G. & Potier, M. (1990). Effects of ionizing radiations on proteins. Evidence of non-random fragmentations and a caution in the use of the method for determination of molecular mass. Biochem. J. 267, 431-439.
    • (1990) Biochem. J. , vol.267 , pp. 431-439
    • Le Maire, M.1    Thauvette, L.2    De Foresta, B.3    Viel, A.4    Beauregard, G.5    Potier, M.6
  • 39
    • 0000478452 scopus 로고    scopus 로고
    • A model of attractive interactions to account for fluid-fluid phase separation of protein solutions
    • Malfois, M., Bonneté, F., Belloni, L. & Tardieu, A. (1996). A model of attractive interactions to account for fluid-fluid phase separation of protein solutions. J. Chem. Phys. 105, 3290-3300.
    • (1996) J. Chem. Phys. , vol.105 , pp. 3290-3300
    • Malfois, M.1    Bonneté, F.2    Belloni, L.3    Tardieu, A.4
  • 40
    • 0025314322 scopus 로고
    • Transmembrane helical interactions and the assembly of the T cell receptor complex
    • Manolios, N., Bonifacino, J. S. & Klausner, R. D. (1990). Transmembrane helical interactions and the assembly of the T cell receptor complex. Science, 249, 274-277.
    • (1990) Science , vol.249 , pp. 274-277
    • Manolios, N.1    Bonifacino, J.S.2    Klausner, R.D.3
  • 43
    • 0015244581 scopus 로고
    • Rhodopsin-like protein from the purple membrane of Halobacterium halobium
    • Oesterhelt, D. & Stoeckenius, W. (1971). Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature New Biol. 233, 149-152.
    • (1971) Nature New Biol. , vol.233 , pp. 149-152
    • Oesterhelt, D.1    Stoeckenius, W.2
  • 44
    • 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
  • 45
    • 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
  • 46
    • 0018632153 scopus 로고
    • Reconstitution, a way of biochemical research; some new approaches to membrane-bound enzymes
    • Racker, E., Violand, B., O'Neal, S., Alfonzo, M. & Telford, J. (1979). Reconstitution, a way of biochemical research; some new approaches to membrane-bound enzymes. Arch. Biochem. Biophys. 198, 470-477.
    • (1979) Arch. Biochem. Biophys. , vol.198 , pp. 470-477
    • Racker, E.1    Violand, B.2    O'Neal, S.3    Alfonzo, M.4    Telford, J.5
  • 47
    • 0017151703 scopus 로고
    • Characterization of membrane proteins in detergent solutions
    • Tanford, C. & Reynolds, J. A. (1976). Characterization of membrane proteins in detergent solutions. Biochim. Biophys. Acta, 457, 133-170.
    • (1976) Biochim. Biophys. Acta , vol.457 , pp. 133-170
    • Tanford, C.1    Reynolds, J.A.2
  • 48
    • 0026554096 scopus 로고
    • Protein interactions in the calf eye lens: Interactions between β-crystallins are repulsive whereas in γ-crystallins they are attractive
    • Tardieu, A., Veretout, F., Krop, B. & Slingsby, C. (1992). Protein interactions in the calf eye lens: interactions between β-crystallins are repulsive whereas in γ-crystallins they are attractive. Eur. Biophys. J. 21, 1-12.
    • (1992) Eur. Biophys. J. , vol.21 , pp. 1-12
    • Tardieu, A.1    Veretout, F.2    Krop, B.3    Slingsby, C.4
  • 49
    • 0025343230 scopus 로고
    • Signal transduction by receptors with tyrosine kinase activity
    • Ullrich, A. & Schlessinger, J. (1990). Signal transduction by receptors with tyrosine kinase activity. Cell, 61, 203-212.
    • (1990) Cell , vol.61 , pp. 203-212
    • Ullrich, A.1    Schlessinger, J.2
  • 50
    • 0017389386 scopus 로고
    • The dimeric nature of the gramicidin A transmembrane channel: Conductance and fluorescence energy transfer studies of hybrid channels
    • Veatch, W. & Stryer, L. (1977). The dimeric nature of the gramicidin A transmembrane channel: conductance and fluorescence energy transfer studies of hybrid channels. J. Mol. Biol. 113, 89-102.
    • (1977) J. Mol. Biol. , vol.113 , pp. 89-102
    • Veatch, W.1    Stryer, L.2
  • 51
    • 0024602852 scopus 로고
    • Molecular basis of eye lens transparency. Osmotic pressure and X-ray analysis of α-crystallin solutions
    • Veretout, F., Delaye, M. & Tardieu, A. (1989). Molecular basis of eye lens transparency. Osmotic pressure and X-ray analysis of α-crystallin solutions. J. Mol. Biol. 205, 713-728.
    • (1989) J. Mol. Biol. , vol.205 , pp. 713-728
    • Veretout, F.1    Delaye, M.2    Tardieu, A.3
  • 52
    • 0028260226 scopus 로고
    • Structural and functional basis for hormone binding and receptor oligomerization
    • Wells, J. A. (1994). Structural and functional basis for hormone binding and receptor oligomerization. Curr. Opin. Cell Biol. 6, 163-173.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 163-173
    • Wells, J.A.1
  • 53
    • 0026729232 scopus 로고
    • Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of X-ray and neutron diffraction data. III. Complete structure
    • Wiener, M. C. & White, S. H. (1992). Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of X-ray and neutron diffraction data. III. Complete structure. Biophys. J. 61, 437-447.
    • (1992) Biophys. J. , vol.61 , pp. 437-447
    • Wiener, M.C.1    White, S.H.2
  • 54
    • 0022438962 scopus 로고
    • Measurement of density and location of solvent associated with biomolecules by small-angle neutron scattering
    • Zaccaï, G. (1986). Measurement of density and location of solvent associated with biomolecules by small-angle neutron scattering. Methods Enzymol. 127, 619-629.
    • (1986) Methods Enzymol. , vol.127 , pp. 619-629
    • Zaccaï, G.1
  • 55
    • 0018792917 scopus 로고
    • Neutron diffraction studies on phosphatidylcholine model membranes. II. Chain conformation and segmental disorder
    • Zaccaï, G., Büldt, G., Seelig, A. & Seelig, J. (1979). Neutron diffraction studies on phosphatidylcholine model membranes. II. Chain conformation and segmental disorder. J. Mol. Biol. 134, 693-706.
    • (1979) J. Mol. Biol. , vol.134 , pp. 693-706
    • Zaccaï, G.1    Büldt, G.2    Seelig, A.3    Seelig, J.4
  • 57
    • 0023042505 scopus 로고
    • Solution structure of halophilic malate dehydrogenase from small-angle neutron and X-ray scattering and ultracentrifugation
    • Zaccaï, G., Wachtel, E. & Eisenberg, H. (1986). Solution structure of halophilic malate dehydrogenase from small-angle neutron and X-ray scattering and ultracentrifugation. J. Mol. Biol. 190, 97-106.
    • (1986) J. Mol. Biol. , vol.190 , pp. 97-106
    • Zaccaï, G.1    Wachtel, E.2    Eisenberg, H.3
  • 58
    • 0021195067 scopus 로고
    • Amino acid, peptide, and protein volume in solution
    • Zamyatnin, A. A. (1984). Amino acid, peptide, and protein volume in solution. Annu. Rev. Biophys. Bioeng. 13, 145-165.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 145-165
    • Zamyatnin, A.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.