메뉴 건너뛰기




Volumn 77, Issue 6, 1999, Pages 3071-3084

Tryptophan octyl ester in detergent micelles of dodecylmaltoside: Fluorescence properties and quenching by brominated detergent analogs

Author keywords

[No Author keywords available]

Indexed keywords

10,11 DIBROMOUNDECANOYL BETA MALTOSIDE; 7,8 DIBROMODODECYL BETA MALTOSIDE; BROMINE DERIVATIVE; DETERGENT; DODECYLMALTOSIDE; MEMBRANE PROTEIN; TRYPTOPHAN OCTYL ESTER; UNCLASSIFIED DRUG;

EID: 0032806293     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77138-9     Document Type: Article
Times cited : (34)

References (59)
  • 1
    • 0026766835 scopus 로고
    • Calibration of the parallax fluorescence quenching method for determination of membrane penetration depth: Refinement and comparison of quenching by spin-labeled and brominated lipids
    • Abrams, F. S., and E. London. 1992. Calibration of the parallax fluorescence quenching method for determination of membrane penetration depth: refinement and comparison of quenching by spin-labeled and brominated lipids. Biochemistry. 31:5312-5322.
    • (1992) Biochemistry , vol.31 , pp. 5312-5322
    • Abrams, F.S.1    London, E.2
  • 2
    • 0024977731 scopus 로고
    • Detergent ringing true as a model for membranes
    • Barber, J. 1989. Detergent ringing true as a model for membranes. Nature. 340:601.
    • (1989) Nature , vol.340 , pp. 601
    • Barber, J.1
  • 3
    • 0014670194 scopus 로고
    • Study of bile salt micelles: Properties of mixed oleate-deoxycholate solutions at pH 9
    • Benzonana, G. 1969. Study of bile salt micelles: properties of mixed oleate-deoxycholate solutions at pH 9. 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
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • Bolen, E. J., and P. W. Holloway. 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
  • 7
    • 0030610813 scopus 로고    scopus 로고
    • b transitions of tryptophan: Applications of theory and experimental observations to fluorescence of proteins
    • b transitions of tryptophan: applications of theory and experimental observations to fluorescence of proteins. Methods Enzymol. 278:113-150.
    • (1997) Methods Enzymol. , vol.278 , pp. 113-150
    • Callis, P.R.1
  • 8
    • 0031274669 scopus 로고    scopus 로고
    • Tryptophan fluorescence shifts in proteins from hybrid simulations: An electrostatic approach
    • Callis, P. R., and B. K. Burgess. 1997. Tryptophan fluorescence shifts in proteins from hybrid simulations: an electrostatic approach. J. Phys. Chem. B. 101:9429-9432.
    • (1997) J. Phys. Chem. B. , vol.101 , pp. 9429-9432
    • Callis, P.R.1    Burgess, B.K.2
  • 9
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • Chattopadhyay, A., and E. London. 1987. Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids. Biochemistry. 26:39-45.
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 10
    • 0030749502 scopus 로고    scopus 로고
    • Ionization, partitioning and dynamics of tryptophan octyl ester: Implications for membrane-bound tryptophan residues
    • Chattopadhyay, A., S. Mukherjee, R. Rukmini, S. S. Rawat, and S. Sudha. 1997. Ionization, partitioning and dynamics of tryptophan octyl ester: implications for membrane-bound tryptophan residues. Biophys. J. 73: 839-849.
    • (1997) Biophys. J. , vol.73 , pp. 839-849
    • Chattopadhyay, A.1    Mukherjee, S.2    Rukmini, R.3    Rawat, S.S.4    Sudha, S.5
  • 11
    • 4644361550 scopus 로고
    • Fluorescence and the structure of proteins. I. Effects of substituents on the fluorescence of indole and phenol compounds
    • Cowgill, R. W. 1963. Fluorescence and the structure of proteins. I. Effects of substituents on the fluorescence of indole and phenol compounds. Arch. Biochem. Biophys. 100:36-44.
    • (1963) Arch. Biochem. Biophys. , vol.100 , pp. 36-44
    • Cowgill, R.W.1
  • 12
    • 0014209817 scopus 로고
    • Fluorescence and protein structure. X. Reappraisal of solvent and structural effects
    • Cowgill, R. W. 1967. Fluorescence and protein structure. X. Reappraisal of solvent and structural effects. Biochim. Biophys. Acta. 133:6-18.
    • (1967) Biochim. Biophys. Acta , vol.133 , pp. 6-18
    • Cowgill, R.W.1
  • 13
    • 0000322550 scopus 로고    scopus 로고
    • Rotational dynamics of lipid/detergent mixtures: A mechanism for membrane protein reconstitution into lipid vesicles
    • Das, T. K. 1996. Rotational dynamics of lipid/detergent mixtures: a mechanism for membrane protein reconstitution into lipid vesicles. J. Phys. Chem. 100:20143-20147.
    • (1996) J. Phys. Chem. , vol.100 , pp. 20143-20147
    • Das, T.K.1
  • 15
    • 0025182226 scopus 로고
    • The role of charge and hydrophobicity in peptide-lipid interaction: A comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers
    • de Kroon, A. I. P. M., M. W. Soekarjo, J. de Gier, and B. De Kruijff. 1990. The role of charge and hydrophobicity in peptide-lipid interaction: a comparative study based on tryptophan fluorescence measurements combined with the use of aqueous and hydrophobic quenchers. Biochemistry. 29:8229-8240.
    • (1990) Biochemistry , vol.29 , pp. 8229-8240
    • De Kroon, A.I.P.M.1    Soekarjo, M.W.2    De Gier, J.3    De Kruijff, B.4
  • 16
    • 0030050146 scopus 로고    scopus 로고
    • Time-resolved fluorescence anisotropy of fluorescent-labeled lysophospholipid and taurodeoxycholate aggregates
    • Delong, L. J., and J. W. Nichols. 1996. Time-resolved fluorescence anisotropy of fluorescent-labeled lysophospholipid and taurodeoxycholate aggregates. Biophys. J. 70:1466-1471.
    • (1996) Biophys. J. , vol.70 , pp. 1466-1471
    • Delong, L.J.1    Nichols, J.W.2
  • 17
    • 0028332128 scopus 로고
    • Uncoupled steps of the colicin A pore formation demonstrated by disulfide bond engineering
    • Duché, D., M. W. Parker, J.-M. González-Mañas, F. Pattus, and D. Baty. 1994. Uncoupled steps of the colicin A pore formation demonstrated by disulfide bond engineering. J. Biol. Chem. 269:6332-6339.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6332-6339
    • Duché, D.1    Parker, M.W.2    González-Mañas, J.-M.3    Pattus, F.4    Baty, D.5
  • 18
    • 0031191278 scopus 로고    scopus 로고
    • Anomeric effects on the structure of micelles of alkyl maltosides in water
    • Dupuy, C., X. Auvray. C. Petipas, I. Rico-Lattes, and A. Lattes. 1997. Anomeric effects on the structure of micelles of alkyl maltosides in water. Langmuir. 13:3965-3967.
    • (1997) Langmuir. , vol.13 , pp. 3965-3967
    • Dupuy, C.1    Auvray, X.2    Petipas, C.3    Rico-Lattes, I.4    Lattes, A.5
  • 19
    • 0020485872 scopus 로고
    • Lipid selectivity of the calcium and magnesium ion dependent adenosine triphosphatase, studied with fluorescence quenching by a brominated phospholipid
    • East, J. M., and A. G. Lee. 1982. Lipid selectivity of the calcium and magnesium ion dependent adenosine triphosphatase, 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
  • 20
    • 0001917250 scopus 로고
    • Fluorescence quenching: Theory and applications
    • J. R. Lakowicz, editor. Plenum Press. New York
    • Eftink, M. R. 1991. Fluorescence quenching: theory and applications. In Topics in Fluorescence Spectroscopy, Vol. 2: Principles. J. R. Lakowicz, editor. Plenum Press. New York, 53-126.
    • (1991) Topics in Fluorescence Spectroscopy, Vol. 2: Principles , vol.2 , pp. 53-126
    • Eftink, M.R.1
  • 21
    • 33847798446 scopus 로고
    • Fluorescence quenching of indole and model micelle systems
    • Eftink, M. R., and C. A. Ghiron. 1976. Fluorescence quenching of indole and model micelle systems. J. Phys. Chem. 80:486-493.
    • (1976) J. Phys. Chem. , vol.80 , pp. 486-493
    • Eftink, M.R.1    Ghiron, C.A.2
  • 22
    • 0027533023 scopus 로고
    • Protein flexibility and aggregation state of human epidermal growth factor, a time resolved fluorescence study of the native protein and engineered single-tryptophan mutants
    • Gallay, J., M. Vincent, I. M. Li de la Sierra, J. Alvarez, R. Ubieta, J. Madrazo, and G. Padron. 1993. Protein flexibility and aggregation state of human epidermal growth factor, a time resolved fluorescence study of the native protein and engineered single-tryptophan mutants. Eur. J. Biochem. 211:213-219.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 213-219
    • Gallay, J.1    Vincent, M.2    Li De La Sierra, I.M.3    Alvarez, J.4    Ubieta, R.5    Madrazo, J.6    Padron, G.7
  • 23
    • 0029901935 scopus 로고    scopus 로고
    • The association of different detergents with the photosynthetic reaction center protein of Rhodobacter sphaeroides R26 and the effects on its photochemistry
    • Gast, P., P. W. Hemelrijk, H. J. Van Gorkom, and A. J. Hoff. 1996. The association of different detergents with the photosynthetic reaction center protein of Rhodobacter sphaeroides R26 and the effects on its photochemistry. Eur. J. Biochem. 239:805-809.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 805-809
    • Gast, P.1    Hemelrijk, P.W.2    Van Gorkom, H.J.3    Hoff, A.J.4
  • 24
    • 0016657917 scopus 로고
    • Solubilization of membranes by detergents
    • Helenius, A., and K. Simons. 1975. Solubilization of membranes by detergents. Biochim. Biophys. Acta. 415:29-79.
    • (1975) Biochim. Biophys. Acta , vol.415 , pp. 29-79
    • Helenius, A.1    Simons, K.2
  • 25
    • 0029895275 scopus 로고    scopus 로고
    • Monomeric human red cell glucose transporter (Glut1) in non-ionic detergent solution and a semi-elliptical torus model for detergent binding to membrane proteins
    • Haneskog, L., L. Andersson, E. Brekkan, A.-K. Englund, K. Kameyama, L. Liljas, E. Greijer, J. Fischbarg, and P. Lundahl. 1996. Monomeric human red cell glucose transporter (Glut1) in non-ionic detergent solution and a semi-elliptical torus model for detergent binding to membrane proteins. Biochim. Biophys. Acta. 1282:39-47.
    • (1996) Biochim. Biophys. Acta , vol.1282 , pp. 39-47
    • Haneskog, L.1    Andersson, L.2    Brekkan, E.3    Englund, A.-K.4    Kameyama, K.5    Liljas, L.6    Greijer, E.7    Fischbarg, J.8    Lundahl, P.9
  • 27
    • 0031770290 scopus 로고    scopus 로고
    • The mechanism of detergent solubilization of liposomes and protein containing membranes
    • Kragh-Hansen, U., M. le Maire, and J. V. Møller. 1998. The mechanism of detergent solubilization of liposomes and protein containing membranes. Biophys. J. 75:2932-2946.
    • (1998) Biophys. J. , vol.75 , pp. 2932-2946
    • Kragh-Hansen, U.1    Le Maire, M.2    Møller, J.V.3
  • 28
    • 0027477920 scopus 로고
    • Transitional steps in the solubilization of protein-containing membranes and liposomes by non-ionic detergent
    • Kragh-Hansen, U., M. le Maire, J. P. Noël, T. Gulik-Kryzwicki, and J. V. Møller. 1993. Transitional steps in the solubilization of protein-containing membranes and liposomes by non-ionic detergent. Biochemistry. 32:1648-1656.
    • (1993) Biochemistry , vol.32 , pp. 1648-1656
    • Kragh-Hansen, U.1    Le Maire, M.2    Noël, J.P.3    Gulik-Kryzwicki, T.4    Møller, J.V.5
  • 29
    • 0024117785 scopus 로고
    • Three-dimensional crystallisation of membrane proteins
    • Kühlbrandt, W. 1988. Three-dimensional crystallisation of membrane proteins. Q. Rev. Biophys. 21:429-477.
    • (1988) Q. Rev. Biophys. , vol.21 , pp. 429-477
    • Kühlbrandt, W.1
  • 30
    • 0029131630 scopus 로고
    • Fluorescence of membrane-bound tryplophan octyl ester: A model for studying intrinsic fluorescence of protein-membrane interactions
    • Ladokhin, A. S., and P. W. Holloway. 1995. Fluorescence of membrane-bound tryplophan octyl ester: a model for studying intrinsic fluorescence of protein-membrane interactions. Biophys. J. 69:506-517.
    • (1995) Biophys. J. , vol.69 , pp. 506-517
    • Ladokhin, A.S.1    Holloway, P.W.2
  • 31
    • 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
  • 32
    • 0021111031 scopus 로고
    • Solubilization of phospholipids by detergents, structural and kinetic aspects
    • Lichtenberg, D., R. J. Robson, and E. A. Dennis. 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
  • 33
    • 0001464493 scopus 로고
    • Analyzing the distribution of decay constants in pulse-fluorimetry using the maximum entropy method
    • Livesey, A. K., and J.-C. Brochon. 1987. Analyzing the distribution of decay constants in pulse-fluorimetry using the maximum entropy method. Biophys. J. 52:693-706.
    • (1987) Biophys. J. , vol.52 , pp. 693-706
    • Livesey, A.K.1    Brochon, J.-C.2
  • 34
    • 0019891873 scopus 로고
    • Fluorescence quenching in model membranes. I. Characterization of quenching caused by a spin-labeled phospholipid
    • London, E., and G. W. Feigenson. 1981. Fluorescence quenching in model membranes. I. Characterization of quenching caused by a spin-labeled phospholipid. Biochemistry. 20:1932-1938.
    • (1981) Biochemistry , vol.20 , pp. 1932-1938
    • London, E.1    Feigenson, G.W.2
  • 36
    • 27844462886 scopus 로고
    • On the nature of the fluorescent state of methylated indole derivatives
    • Meech, S. R., D. Phillips, and A. G. Lee. 1983. On the nature of the fluorescent state of methylated indole derivatives. Chem. Phys. 80: 317-328.
    • (1983) Chem. Phys. , vol.80 , pp. 317-328
    • Meech, S.R.1    Phillips, D.2    Lee, A.G.3
  • 37
    • 0029761131 scopus 로고    scopus 로고
    • 2 and class Y amphipathic helical peptides with membranes
    • 2 and class Y amphipathic helical peptides with membranes. Biochemistry. 35:11210-11220.
    • (1996) Biochemistry , vol.35 , pp. 11210-11220
    • Mishra, V.K.1    Palgunachari, M.N.2
  • 38
    • 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
  • 39
    • 0000559797 scopus 로고
    • Uses of non-ionic and bile salt detergents in the study of membrane proteins
    • A. Watts and J. J. H. H. M. De Pont, editors. Elsiever Science Publishers BV, Amsterdam
    • Møller, J. V., M. le Maire, and J. P. Andersen. 1986. Uses of non-ionic and bile salt detergents in the study of membrane proteins. In Progress in Protein-Lipid Interactions Vol. 2. A. Watts and J. J. H. H. M. De Pont, editors. Elsiever Science Publishers BV, Amsterdam. 147-196.
    • (1986) Progress in Protein-Lipid Interactions , vol.2 , pp. 147-196
    • Møller, J.V.1    Le Maire, M.2    Andersen, J.P.3
  • 40
    • 0024291653 scopus 로고
    • Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared by reverse-phase evaporation) by Triton X-100, octyl glucoside, and sodium cholate
    • Paternostre, M.-T., M. Roux, and J.-L Rigaud. 1988. Mechanisms of membrane protein insertion into liposomes during reconstitution procedures involving the use of detergents. 1. Solubilization of large unilamellar liposomes (prepared 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
  • 43
    • 0020763601 scopus 로고
    • On the origin of nonexponential fluorescence decay in tryptophan and its derivatives
    • Petrich, J. W., M. C. Chang, D. B. McDonald, and G. R. Fleming. 1983. On the origin of nonexponential fluorescence decay in tryptophan and its derivatives. J. Am. Chem. Soc. 105:3824-3832.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3824-3832
    • Petrich, J.W.1    Chang, M.C.2    McDonald, D.B.3    Fleming, G.R.4
  • 44
    • 0000058811 scopus 로고    scopus 로고
    • Micellar organization and dynamics: A wavelength fluorescence approach
    • Rawat, S. S., S. Mukherjee, and A. Chattopadhyay. 1997. Micellar organization and dynamics: a wavelength fluorescence approach. J. Phys. Chem. 101:1922-1929.
    • (1997) J. Phys. Chem. , vol.101 , pp. 1922-1929
    • Rawat, S.S.1    Mukherjee, S.2    Chattopadhyay, A.3
  • 45
    • 0030738720 scopus 로고    scopus 로고
    • Transmembrane orientation of hydrophobic α-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration
    • Ren, J., S. Lew, Z. Wang, and E. London. 1997. Transmembrane orientation of hydrophobic α-helices is regulated both by the relationship of helix length to bilayer thickness and by the cholesterol concentration. Biochemistry. 36:10213-10220.
    • (1997) Biochemistry , vol.36 , pp. 10213-10220
    • Ren, J.1    Lew, S.2    Wang, Z.3    London, E.4
  • 46
    • 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., B. Arnoux, A. Ducruix, and F. Reiss-Husson. 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
  • 47
  • 48
    • 0030909560 scopus 로고    scopus 로고
    • Immuno-suppressor binding to the immunophilin fkbp59 affects the local structural dynamics of a surface β-strand: Time-resolved fluorescence study
    • Rouvière, N., M. Vincent, C. T. Craescu, and J. Gallay. 1997. Immuno-suppressor binding to the immunophilin FKBP59 affects the local structural dynamics of a surface β-strand: time-resolved fluorescence study. Biochemistry. 36:7339-7352.
    • (1997) Biochemistry , vol.36 , pp. 7339-7352
    • Rouvière, N.1    Vincent, M.2    Craescu, C.T.3    Gallay, J.4
  • 50
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • Szabo, A. G., and D. M. Rayner. 1980. Fluorescence decay of tryptophan conformers in aqueous solution. J. Am. Chem. Soc. 102:554-563.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 554-563
    • Szabo, A.G.1    Rayner, D.M.2
  • 51
    • 0017151703 scopus 로고
    • Characterization of membrane proteins in detergent solutions
    • Tanford, C., and J. A. Reynolds. 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
  • 53
    • 0026777830 scopus 로고
    • Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding
    • Ulbrandt, N. D., E. London, and D. B. Oliver. 1992. Deep penetration of a portion of Escherichia coli SecA protein into model membranes is promoted by anionic phospholipids and by partial unfolding. J. Biol. Chem. 267:15184-15192.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15184-15192
    • Ulbrandt, N.D.1    London, E.2    Oliver, D.B.3
  • 55
    • 0031047828 scopus 로고    scopus 로고
    • Conformational changes due to membrane binding and channel formation by staphylococcal α-toxin
    • Vécsey-Semjén, B., C. Lesieur, R. Möllby, and F. G. van der Goot. 1997. Conformational changes due to membrane binding and channel formation by staphylococcal α-toxin. J. Biol. Chem. 272:5709-5717.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5709-5717
    • Vécsey-Semjén, B.1    Lesieur, C.2    Möllby, R.3    Van Der Goot, F.G.4
  • 56
    • 33751156520 scopus 로고
    • Solvent relaxation around the excited state of indole: Analysis of fluorescence lifetime distributions and time-dependence spectral shifts
    • Vincent, M., J. Gallay, and A. P. Demchenko. 1995. Solvent relaxation around the excited state of indole: analysis of fluorescence lifetime distributions and time-dependence spectral shifts. J. Phys. Chem. 99: 14931-14941.
    • (1995) J. Phys. Chem. , vol.99 , pp. 14931-14941
    • Vincent, M.1    Gallay, J.2    Demchenko, A.P.3
  • 57
    • 0024745128 scopus 로고
    • Vesicle-micelle transition of phosphatidylcholine and octyl glucoside elucidated by cryo-transmission electron microscopy
    • Vinson, P. K., Y. Talmon, and A. Walter. 1989. Vesicle-micelle transition of phosphatidylcholine and octyl glucoside elucidated by cryo-transmission electron microscopy. Biophys. J. 56:669-681.
    • (1989) Biophys. J. , vol.56 , pp. 669-681
    • Vinson, P.K.1    Talmon, Y.2    Walter, A.3
  • 58
    • 0030698195 scopus 로고    scopus 로고
    • Ligand-induced movement of helix X in the lactose permease from Escherichia coli: A fluorescence quenching study
    • Wang, Q., K. Matsushita, B. de Foresta, M. le Maire, and H. R. Kaback. 1997. Ligand-induced movement of helix X in the lactose permease from Escherichia coli: a fluorescence quenching study. Biochemistry. 36:14120-14127.
    • (1997) Biochemistry , vol.36 , pp. 14120-14127
    • Wang, Q.1    Matsushita, K.2    De Foresta, B.3    Le Maire, M.4    Kaback, H.R.5
  • 59
    • 0025281427 scopus 로고
    • Fluorescence quenching in model membranes: Phospholipid acyl chain distributions around small fluorophores
    • Yeager, M. D., and G. W. Feigenson. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.