메뉴 건너뛰기




Volumn 241, Issue 2, 1996, Pages 343-354

Brominated detergents as tools to study protein-detergent interactions

Author keywords

2 O lauroylsucrose; Brominated detergent; Fluorescence quenching; n dodecyl D maltoside; Protein detergent interactions

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DETERGENT; MEMBRANE PROTEIN; ORGANOBROMINE DERIVATIVE;

EID: 0029961288     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00343.x     Document Type: Article
Times cited : (25)

References (69)
  • 2
    • 0028924959 scopus 로고
    • 2+-ATPase of sarcoplasmic reticulum
    • 2+-ATPase of sarcoplasmic reticulum, J. Biol. Chem. 270, 908-914.
    • (1995) J. Biol. Chem. , vol.270 , pp. 908-914
    • Andersen, J.P.1
  • 3
    • 0014670194 scopus 로고
    • Study of bile salts micelles: Properties of mixed oleate-deoxycholate solutions at pH 9.0
    • Benzonana, G. (1969) Study of bile salts micelles: properties of mixed oleate-deoxycholate solutions at pH 9.0, Biochim. Biophys. Acta 176, 836-848.
    • (1969) Biochim. Biophys. Acta , vol.176 , pp. 836-848
    • Benzonana, G.1
  • 4
    • 0001018071 scopus 로고
    • Empirical study of heavy-atom collisional quenching of the fluorescence state of aromatic compounds in solution
    • Berlman, I. B. (1973) Empirical study of heavy-atom collisional quenching of the fluorescence state of aromatic compounds in solution, J. Phys. Chem. 77, 562-567.
    • (1973) J. Phys. Chem. , vol.77 , pp. 562-567
    • Berlman, I.B.1
  • 5
    • 0023651702 scopus 로고
    • Preferential lipid association and mode of penetration of apocytochrome c in mixed model membranes as monitored by tryptophanyl fluorescence quenching using brominated phospholipids
    • Berkhout, T. A., Rietveld, A. & de Kruijff, B. (1987) Preferential lipid association and mode of penetration of apocytochrome c in mixed model membranes as monitored by tryptophanyl fluorescence quenching using brominated phospholipids, Biochim. Biophys. Acta 897, 1-4.
    • (1987) Biochim. Biophys. Acta , vol.897 , pp. 1-4
    • Berkhout, T.A.1    Rietveld, A.2    De Kruijff, B.3
  • 6
    • 0021765180 scopus 로고
    • Fluorescence characterisation of the low pH-induced change in diphtheria toxin conformation: Effect of salt
    • Blewitt, M. G., Zhao, J. M., McKeever, B., Sarma, R. & London, E. (1984) Fluorescence characterisation of the low pH-induced change in diphtheria toxin conformation: effect of salt, Biochem. Biophys. Res. Commun. 120, 286-290.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 286-290
    • Blewitt, M.G.1    Zhao, J.M.2    McKeever, B.3    Sarma, R.4    London, E.5
  • 7
    • 0022425596 scopus 로고
    • Characterization of a spinach photosystem II core preparation isolated by a simplified method
    • Bricker, T. M., Pakrasi, H. B. & Sherman, L. A. (1985) Characterization of a spinach photosystem II core preparation isolated by a simplified method, Arch. Biochem. Biophys. 237, 170-176.
    • (1985) Arch. Biochem. Biophys. , vol.237 , pp. 170-176
    • Bricker, T.M.1    Pakrasi, H.B.2    Sherman, L.A.3
  • 8
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • Bolen, E. J. & Holloway, P. W. (1990) Quenching of tryptophan fluorescence by brominated phospholipid, Biochemistry 29, 9638-9643.
    • (1990) Biochemistry , vol.29 , pp. 9638-9643
    • Bolen, E.J.1    Holloway, P.W.2
  • 9
    • 0021915284 scopus 로고
    • Interaction of magnesium and inorganic phosphate with calcium-deprived sarcoplasmic reticulum adenosinetriphosphatase as reflected by organic solvent induced perturbation
    • Champeil, P., Guillain, F., Vénien, C. & Gingold, M. P. (1985) Interaction of magnesium and inorganic phosphate with calcium-deprived sarcoplasmic reticulum adenosinetriphosphatase as reflected by organic solvent induced perturbation, Biochemistry 24, 69-81.
    • (1985) Biochemistry , vol.24 , pp. 69-81
    • Champeil, P.1    Guillain, F.2    Vénien, C.3    Gingold, M.P.4
  • 10
    • 0022914647 scopus 로고
    • Kinetic characterization of the normal and detergent-perturbed reaction cycles of the sarcoplasmic reticulum calcium pump. Rate limiting steps under different conditions
    • Champeil, P., le Maire, M., Andersen, J. P., Guillain, F., Gingold, M., Lund, S. & Møller, J. V. (1986) Kinetic characterization of the normal and detergent-perturbed reaction cycles of the sarcoplasmic reticulum calcium pump. Rate limiting steps under different conditions, J. Biol. Chem. 261, 16372-16384.
    • (1986) J. Biol. Chem. , vol.261 , pp. 16372-16384
    • Champeil, P.1    Le Maire, M.2    Andersen, J.P.3    Guillain, F.4    Gingold, M.5    Lund, S.6    Møller, J.V.7
  • 11
    • 0023430247 scopus 로고
    • Isoparametric analysis of binding and partitioning processes
    • Chatelier, R. C. & Sawyer, W. H. (1987) Isoparametric analysis of binding and partitioning processes, J. Biochem. Biophys. Methods 15, 49-61.
    • (1987) J. Biochem. Biophys. Methods , vol.15 , pp. 49-61
    • Chatelier, R.C.1    Sawyer, W.H.2
  • 13
    • 33751386123 scopus 로고
    • New highly regioselective reactions of unprotected sucrose. Synthesis of 2-O-acylsucroses and 2-O-(N-alkylcarbamoyl)sucroses
    • Chauvin, C., Baczko, K. & Plusquellec, D. (1993a) New highly regioselective reactions of unprotected sucrose. Synthesis of 2-O-acylsucroses and 2-O-(N-alkylcarbamoyl)sucroses, J. Org. Chem. 58, 2291-2295.
    • (1993) J. Org. Chem. , vol.58 , pp. 2291-2295
    • Chauvin, C.1    Baczko, K.2    Plusquellec, D.3
  • 14
    • 21144483888 scopus 로고
    • Differentiation of regioisomeric esters of sucrose by ionspray tandem mass spectrometry
    • Chauvin, C., Thibault, P., Plusquellec, D. & Banoub, J. (1993b) Differentiation of regioisomeric esters of sucrose by ionspray tandem mass spectrometry, J. Carbohydr. Chem. 12, 459-475.
    • (1993) J. Carbohydr. Chem. , vol.12 , pp. 459-475
    • Chauvin, C.1    Thibault, P.2    Plusquellec, D.3    Banoub, J.4
  • 15
    • 0025738363 scopus 로고
    • Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli
    • Davidson, A. L. & Nikaido, H. (1991) Purification and characterization of the membrane-associated components of the maltose transport system from Escherichia coli, J. Biol. Chem. 266, 8946-8951.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8946-8951
    • Davidson, A.L.1    Nikaido, H.2
  • 16
    • 33845379843 scopus 로고
    • Surface properties and micellar interfacial microenvironment of n-dodecyl β-D-maltoside
    • Drummond, C. J., Warr, G. G., Grieser, F., Ninham, B. W. & Evans, D. F. (1985) Surface properties and micellar interfacial microenvironment of n-dodecyl β-D-maltoside, J. Phys. Chem. 89, 2103-2109.
    • (1985) J. Phys. Chem. , vol.89 , pp. 2103-2109
    • Drummond, C.J.1    Warr, G.G.2    Grieser, F.3    Ninham, B.W.4    Evans, D.F.5
  • 17
    • 0020485872 scopus 로고
    • Lipid selectivity of the calcium and magnesium ion dependent adenosinetriphosphatase, studied with fluorescence quenching by a brominated phospholipid
    • East, J. M. & Lee, A. G. (1982) Lipid selectivity of the calcium and magnesium ion dependent adenosinetriphosphatase, studied with fluorescence quenching by a brominated phospholipid, Biochemistry 21, 4144-4151.
    • (1982) Biochemistry , vol.21 , pp. 4144-4151
    • East, J.M.1    Lee, A.G.2
  • 22
    • 0025148798 scopus 로고
    • How to evaluate the distribution of an 'invisible' amphiphile between biological membranes and water
    • de Foresta, B., Merah, Z., le Maire, M. & Champeil, P. (1990b) How to evaluate the distribution of an 'invisible' amphiphile between biological membranes and water, Anal. Biochem. 189, 59-67.
    • (1990) Anal. Biochem. , vol.189 , pp. 59-67
    • De Foresta, B.1    Merah, Z.2    Le Maire, M.3    Champeil, P.4
  • 25
    • 10244231817 scopus 로고    scopus 로고
    • Brominated detergents for structural studies of membrane proteins
    • de Foresta, B., Champeil, P. & le Maire, M. (1996) Brominated detergents for structural studies of membrane proteins, Biophys. J. 70, A208.
    • (1996) Biophys. J. , vol.70
    • De Foresta, B.1    Champeil, P.2    Le Maire, M.3
  • 27
    • 0018278640 scopus 로고
    • Surface density determination in membranes by fluorescence energy transfer
    • Fung, B. K. & Stryer, L. (1978) Surface density determination in membranes by fluorescence energy transfer, Biochemistry 17, 5241-5248.
    • (1978) Biochemistry , vol.17 , pp. 5241-5248
    • Fung, B.K.1    Stryer, L.2
  • 28
    • 0024794115 scopus 로고
    • ATP-driven cation pumps: Alignment of sequences
    • Green, N. M. (1989) ATP-driven cation pumps: alignment of sequences, Biochem. Soc. Trans. 17, 972.
    • (1989) Biochem. Soc. Trans. , vol.17 , pp. 972
    • Green, N.M.1
  • 29
    • 0026759604 scopus 로고
    • Brominated phospholipids as a tool for monitoring the membrane insertion of colicin A
    • González-Mañas, J. M., Lakey, J. H. & Pattus, F. (1992) Brominated phospholipids as a tool for monitoring the membrane insertion of colicin A, Biochemistry 31, 7294-7300.
    • (1992) Biochemistry , vol.31 , pp. 7294-7300
    • González-Mañas, J.M.1    Lakey, J.H.2    Pattus, F.3
  • 30
    • 0024595001 scopus 로고
    • Characterization of the tryptophan fluorescence from sarcoplasmic reticulum adenosinetriphosphatase by frequency-domain fluorescence spectroscopy
    • Gryczynski, I., Wiczk, W., Inesi, G., Squier, T. & Lakowicz, J. R. (1989) Characterization of the tryptophan fluorescence from sarcoplasmic reticulum adenosinetriphosphatase by frequency-domain fluorescence spectroscopy, Biochemistry 28, 3490-3498.
    • (1989) Biochemistry , vol.28 , pp. 3490-3498
    • Gryczynski, I.1    Wiczk, W.2    Inesi, G.3    Squier, T.4    Lakowicz, J.R.5
  • 31
    • 0026045374 scopus 로고
    • Kinetic characterization of the normal and procaine-perturbed reaction cycles of the sarcoplasmic reticulum calcium pump
    • Henao, F., de Foresta, B., Orlowski, S., Cuenda, A., Gutierrez-Merino, C. & Champeil, P. (1991) Kinetic characterization of the normal and procaine-perturbed reaction cycles of the sarcoplasmic reticulum calcium pump, Eur. J. Biochem. 202, 559-567.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 559-567
    • Henao, F.1    De Foresta, B.2    Orlowski, S.3    Cuenda, A.4    Gutierrez-Merino, C.5    Champeil, P.6
  • 33
    • 0025273607 scopus 로고
    • High-resolution electron density profiles reveal influence of fatty acids on bilayer structure
    • Katsaras, J. & Stinson, R. H. (1990) High-resolution electron density profiles reveal influence of fatty acids on bilayer structure. Biophys. J. 57, 649-655.
    • (1990) Biophys. J. , vol.57 , pp. 649-655
    • Katsaras, J.1    Stinson, R.H.2
  • 34
    • 0028068353 scopus 로고
    • Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity
    • Kessi, J., Poirée, J.-C., Wehrli, E., Bachofen, R., Semenza, G. & Hauser, H. (1994) Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity. Biochemistry 33, 10825-10836.
    • (1994) Biochemistry , vol.33 , pp. 10825-10836
    • Kessi, J.1    Poirée, J.-C.2    Wehrli, E.3    Bachofen, R.4    Semenza, G.5    Hauser, H.6
  • 35
    • 0021395384 scopus 로고
    • Activation volumes of the calcium dependent para-nitrophenyl phosphate hydrolysis of the sarcoplasmic reticulum calcium transport enzyme
    • König, K. G. & Hasselbach, W. (1984) Activation volumes of the calcium dependent para-nitrophenyl phosphate hydrolysis of the sarcoplasmic reticulum calcium transport enzyme, Z. Naturforsch. 39c, 282-284.
    • (1984) Z. Naturforsch. , vol.39 C , pp. 282-284
    • König, K.G.1    Hasselbach, W.2
  • 36
    • 0027477920 scopus 로고
    • Transitional steps in the solubilization of protein-containing membranes and liposomes by nonionic detergents
    • Kragh-Hansen, U., le Maire, M., Nöel, J. P., Gulik-Krzywicki, T. & Møller, J. V. (1993) Transitional steps in the solubilization of protein-containing membranes and liposomes by nonionic detergents, Biochemistry 32, 1648-1656.
    • (1993) Biochemistry , vol.32 , pp. 1648-1656
    • Kragh-Hansen, U.1    Le Maire, M.2    Nöel, J.P.3    Gulik-Krzywicki, T.4    Møller, J.V.5
  • 37
    • 0024117785 scopus 로고
    • Three-dimensional crystallization of membrane proteins
    • Kühlbrandt, W. (1988) Three-dimensional crystallization of membrane proteins, Q. Rev. Biophys. 21, 429-477.
    • (1988) Q. Rev. Biophys. , vol.21 , pp. 429-477
    • Kühlbrandt, W.1
  • 39
    • 0023666958 scopus 로고
    • Binding of a nonionic detergent to membranes: Flip-flop rate and location on the bilayer
    • le Maire, M., Møller, J. V. & Champeil, P. (1987) Binding of a nonionic detergent to membranes: flip-flop rate and location on the bilayer. Biochemistry 26, 4803-4810.
    • (1987) Biochemistry , vol.26 , pp. 4803-4810
    • Le Maire, M.1    Møller, J.V.2    Champeil, P.3
  • 40
    • 77957091108 scopus 로고    scopus 로고
    • 2+-ATPase
    • Lee, A. G., ed. Jai Press, Greenwich CT
    • 2+-ATPase, in Biomembranes, vol. 5 (Lee, A. G., ed.) pp. 1-42, Jai Press, Greenwich CT.
    • (1996) Biomembranes , vol.5 , pp. 1-42
    • Lee, A.G.1
  • 42
    • 0021111031 scopus 로고
    • Solubilization of phospholipids by detergents. Structural and kinetic aspects
    • Lichtenberg, D., Robson, R. J. & Dennis, E. A. (1983) Solubilization of phospholipids by detergents. Structural and kinetic aspects, Biochim. Biophys. Acta 737, 285-304.
    • (1983) Biochim. Biophys. Acta , vol.737 , pp. 285-304
    • Lichtenberg, D.1    Robson, R.J.2    Dennis, E.A.3
  • 43
    • 0022348630 scopus 로고
    • Characterization of the solubilization of lipid bilayers by surfactants
    • Lichtenberg, D. (1985) Characterization of the solubilization of lipid bilayers by surfactants, Biochim. Biophys. Acta 821, 470-478.
    • (1985) Biochim. Biophys. Acta , vol.821 , pp. 470-478
    • Lichtenberg, D.1
  • 44
    • 0021180134 scopus 로고
    • Interaction of chlorpromazine with the human erythrocyte membrane
    • Lieber, M. R., Lange, Y., Weinstein, R. S. & Steck, T. (1984) Interaction of chlorpromazine with the human erythrocyte membrane, J. Biol. Chem. 259, 9225-9234.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9225-9234
    • Lieber, M.R.1    Lange, Y.2    Weinstein, R.S.3    Steck, T.4
  • 45
    • 0022459925 scopus 로고
    • A fluorescence-based detergent binding assay for protein hydrophobicity
    • London, E. (1986) A fluorescence-based detergent binding assay for protein hydrophobicity. Anal. Biochem. 154, 57-63.
    • (1986) Anal. Biochem. , vol.154 , pp. 57-63
    • London, E.1
  • 47
    • 0022371456 scopus 로고
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence
    • 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence, Nature 316, 696-700.
    • (1985) Nature , vol.316 , pp. 696-700
    • MacLennan, D.H.1    Brandi, C.J.2    Korczak, B.3    Green, N.M.4
  • 49
    • 0023111150 scopus 로고
    • Determination of the depth of bromine atoms in bilayers formed from bromolipid probes
    • McIntosh, T. J. & Holloway, P. W. (1987) Determination of the depth of bromine atoms in bilayers formed from bromolipid probes. Biochemistry 26, 1783-1788.
    • (1987) Biochemistry , vol.26 , pp. 1783-1788
    • McIntosh, T.J.1    Holloway, P.W.2
  • 51
    • 0027283560 scopus 로고
    • Detergent binding as a measure of hydrophobic surface area of integral membrane proteins
    • Møller, J. V. & le Maire, M. (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
    • 0000559797 scopus 로고
    • Uses of non-ionic and bile salt detergents in the study of membrane proteins
    • (Watts, A. & DePont, J. J. H. H. M., eds) ch. 2, Elsevier Science Publishers BV. Amsterdam
    • Møller, J. V., le Maire, M. & Andersen, J. P. (1986) Uses of non-ionic and bile salt detergents in the study of membrane proteins, in Progress in protein-lipid interactions (Watts, A. & DePont, J. J. H. H. M., eds) ch. 2, pp. 147-196, Elsevier Science Publishers BV. Amsterdam.
    • (1986) Progress in Protein-lipid Interactions , pp. 147-196
    • Møller, J.V.1    Le Maire, M.2    Andersen, J.P.3
  • 53
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Møller, J. V., Juul, B. & le Maire, M. (1996) Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta 1286, 1-51.
    • (1996) Biochim. Biophys. Acta , vol.1286 , pp. 1-51
    • Møller, J.V.1    Juul, B.2    Le Maire, M.3
  • 54
    • 0024281314 scopus 로고
    • Micellevesicle transition of egg phosphatidylcholine and octyl glucoside
    • Ollivon, M., Eidelman, O., Blumenthal, R. & Walter, A. (1988) Micellevesicle transition of egg phosphatidylcholine and octyl glucoside, Biochemistry 27, 1695-1703.
    • (1988) Biochemistry , vol.27 , pp. 1695-1703
    • Ollivon, M.1    Eidelman, O.2    Blumenthal, R.3    Walter, A.4
  • 55
    • 0024291653 scopus 로고
    • Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1-Solubilization of large unilamellar liposomes (performed by reverse-phase evaporation) by Triton X-100, octyl glucoside and sodium cholate
    • Paternostre, M.-T., Roux, M. & Rigaud, J.-L. (1988) Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1-Solubilization of large unilamellar liposomes (performed by reverse-phase evaporation) by Triton X-100, octyl glucoside and sodium cholate. Biochemistry 27, 2668-2677.
    • (1988) Biochemistry , vol.27 , pp. 2668-2677
    • Paternostre, M.-T.1    Roux, M.2    Rigaud, J.-L.3
  • 57
    • 0023769532 scopus 로고
    • Solubilization and hydrodynamic properties of pig atrial muscarinic acetylcholine receptor in dodecyl β-D-maltoside
    • Peterson, G. L., Rosenbaum, L. C. & Schimerlik, M. I. (1988) Solubilization and hydrodynamic properties of pig atrial muscarinic acetylcholine receptor in dodecyl β-D-maltoside, Biochem. J. 255, 553-560.
    • (1988) Biochem. J. , vol.255 , pp. 553-560
    • Peterson, G.L.1    Rosenbaum, L.C.2    Schimerlik, M.I.3
  • 58
    • 0022411967 scopus 로고
    • Influence of detergent polar and apolar structure upon the temperature dependence of beef heart cytochrome c oxidase activity
    • Robinson, N. C., Neumann, J. & Wiginton, D. (1985) Influence of detergent polar and apolar structure upon the temperature dependence of beef heart cytochrome c oxidase activity, Biocheinixtry 24, 6298-6304.
    • (1985) Biocheinixtry , vol.24 , pp. 6298-6304
    • Robinson, N.C.1    Neumann, J.2    Wiginton, D.3
  • 59
    • 0019328971 scopus 로고
    • Alkyl glycoside detergents: A simpler synthesis and their effects on kinetic and physical properties of cytochrome c oxidase
    • Rosevear, P., VanAken, T., Baxter, J. & Ferguson-Miller, S. (1980) Alkyl glycoside detergents: a simpler synthesis and their effects on kinetic and physical properties of cytochrome c oxidase, Biochemistry 19, 4108-4115.
    • (1980) Biochemistry , vol.19 , pp. 4108-4115
    • Rosevear, P.1    VanAken, T.2    Baxter, J.3    Ferguson-Miller, S.4
  • 60
    • 0025736558 scopus 로고
    • 2+-ATPase by active site cross-linking: Impairment of nucleotide binding slows nucleotide-dependent phosphoryl transfer and loss of active site flexibility stabilizes occluded forms and blocks E2-P formation
    • 2+-ATPase by active site cross-linking: impairment of nucleotide binding slows nucleotide-dependent phosphoryl transfer and loss of active site flexibility stabilizes occluded forms and blocks E2-P formation, J. Biol. Chem. 266, 4613-4621.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4613-4621
    • Ross, D.C.1    Davidson, G.A.2    McIntosh, D.B.3
  • 61
    • 0025990887 scopus 로고
    • Structure of the detergent phase and protein-detergent interactions in crystals of the wild-type (strain Y) Rhodobacter sphaeroides photochemical reaction center
    • Roth, M., Arnoux, B., Ducruix, A. & Reiss-Husson, F. (1991) Structure of the detergent phase and protein-detergent interactions in crystals of the wild-type (strain Y) Rhodobacter sphaeroides photochemical reaction center, Biochemistry 30, 9403-9413.
    • (1991) Biochemistry , vol.30 , pp. 9403-9413
    • Roth, M.1    Arnoux, B.2    Ducruix, A.3    Reiss-Husson, F.4
  • 62
    • 0001591631 scopus 로고
    • Membrane fluidity and cellular functions
    • Shinitzky, M., ed. CRC Press, Boca Raton FL
    • Shinitzky, M. (1984) Membrane fluidity and cellular functions in Physiology of membrane fluidity (Shinitzky, M., ed.) pp. 1-52, CRC Press, Boca Raton FL.
    • (1984) Physiology of Membrane Fluidity , pp. 1-52
    • Shinitzky, M.1
  • 66
    • 0026045166 scopus 로고
    • Photosystem II panicles from Chlamydomonas reinhardtii. Purification, molecular weight, small subunit composition, and protein phosphorylation
    • de Vitry, C., Diner, B. A. & Popot, J. L. (1991) Photosystem II panicles from Chlamydomonas reinhardtii. Purification, molecular weight, small subunit composition, and protein phosphorylation, J. Biol. Chem. 266, 16614-16621.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16614-16621
    • De Vitry, C.1    Diner, B.A.2    Popot, J.L.3
  • 67
    • 0025819980 scopus 로고
    • Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analogue of dioleoylphosphatidylcholine
    • Wiener, M. C. & White, S. H. (1991) Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analogue of dioleoylphosphatidylcholine, Biochemistry 30, 6997-7008.
    • (1991) Biochemistry , vol.30 , pp. 6997-7008
    • Wiener, M.C.1    White, S.H.2
  • 68
    • 0025281427 scopus 로고
    • Fluorescence quenching in model membranes: Phospholipid acyl chain distributions around small fluorophores
    • Yeager, M. D. & Feigenson, G. W. (1990) Fluorescence quenching in model membranes: phospholipid acyl chain distributions around small fluorophores, Biochemistry 29, 4380-4392.
    • (1990) Biochemistry , vol.29 , pp. 4380-4392
    • Yeager, M.D.1    Feigenson, G.W.2
  • 69
    • 0023696942 scopus 로고
    • Conformation and model membrane interactions of diphtheria toxin fragment A
    • Zhao, J. M. & London, E. (1988) Conformation and model membrane interactions of diphtheria toxin fragment A. J. Biol. Chem. 263, 15369-15377.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15369-15377
    • Zhao, J.M.1    London, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.