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Volumn 121, Issue 3, 2006, Pages 218-223

Conformational changes of β-lactoglobulin induced by anionic phospholipid

Author keywords

lactoglobulin; Circular dichroism; Conformational changes; DMPG; Fluorescence; UV VIS

Indexed keywords

BETA LACTOGLOBULIN; DIMYRISTOYLPHOSPHATIDYLGLYCEROL; PHOSPHOLIPID;

EID: 33646889069     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2005.12.015     Document Type: Article
Times cited : (49)

References (30)
  • 1
    • 0032498226 scopus 로고    scopus 로고
    • Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy
    • Arai M., Ikura T., Semisotnov G.V., Kihara H., Amemiya Y., and Kuwajima K. Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy. J. Mol. Biol. 275 (1998) 149-162
    • (1998) J. Mol. Biol. , vol.275 , pp. 149-162
    • Arai, M.1    Ikura, T.2    Semisotnov, G.V.3    Kihara, H.4    Amemiya, Y.5    Kuwajima, K.6
  • 3
    • 0032004945 scopus 로고    scopus 로고
    • Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies
    • Renard D., Lefebvre J., Griffin M.C.A., and Griffin W.G. Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies. Int. J. Biol. Macromol. 22 (1998) 41-49
    • (1998) Int. J. Biol. Macromol. , vol.22 , pp. 41-49
    • Renard, D.1    Lefebvre, J.2    Griffin, M.C.A.3    Griffin, W.G.4
  • 6
    • 0032741871 scopus 로고    scopus 로고
    • Solution structure and dynamics of bovine beta-lactoglobulin A
    • Kuwata K., Hoshino M., Forge V., Era S., Batt C.A., and Goto Y. Solution structure and dynamics of bovine beta-lactoglobulin A. Protein Sci. 8 (1999) 2541-2545
    • (1999) Protein Sci. , vol.8 , pp. 2541-2545
    • Kuwata, K.1    Hoshino, M.2    Forge, V.3    Era, S.4    Batt, C.A.5    Goto, Y.6
  • 7
    • 0032923417 scopus 로고    scopus 로고
    • Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin
    • Qin B.Y., Bewley M.C., Creamer L.K., Baker E.N., and Jameson G.B. Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin. Protein Sci. 8 (1999) 75-83
    • (1999) Protein Sci. , vol.8 , pp. 75-83
    • Qin, B.Y.1    Bewley, M.C.2    Creamer, L.K.3    Baker, E.N.4    Jameson, G.B.5
  • 8
    • 0032110129 scopus 로고    scopus 로고
    • Complete assignment of H-1, C-13 and N-15 chemical shifts for bovine beta-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form
    • Uhrinova S., Uhrin D., Denton H., Smith M., Sawyer L., and Barlow N. Complete assignment of H-1, C-13 and N-15 chemical shifts for bovine beta-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form. J. Biomol. NMR 12 (1998) 89-107
    • (1998) J. Biomol. NMR , vol.12 , pp. 89-107
    • Uhrinova, S.1    Uhrin, D.2    Denton, H.3    Smith, M.4    Sawyer, L.5    Barlow, N.6
  • 9
    • 0035839994 scopus 로고    scopus 로고
    • Conformational rearrangement of beta-lactoglobulin upon interaction with an anionic membrane
    • Lefevre T., and Subirade M. Conformational rearrangement of beta-lactoglobulin upon interaction with an anionic membrane. Biochim. Biophys. Acta 1549 (2001) 37-50
    • (2001) Biochim. Biophys. Acta , vol.1549 , pp. 37-50
    • Lefevre, T.1    Subirade, M.2
  • 11
    • 0031004544 scopus 로고    scopus 로고
    • The application of circular dichroism to studies of protein folding and unfolding
    • Kelly S.M., and Price N.C. The application of circular dichroism to studies of protein folding and unfolding. Biochim. Biophys. Acta 1338 (1997) 161-185
    • (1997) Biochim. Biophys. Acta , vol.1338 , pp. 161-185
    • Kelly, S.M.1    Price, N.C.2
  • 12
    • 0035824880 scopus 로고    scopus 로고
    • Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies
    • Taulier N., and Chalikian T.V. Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies. J. Mol. Biol. 314 (2001) 873-889
    • (2001) J. Mol. Biol. , vol.314 , pp. 873-889
    • Taulier, N.1    Chalikian, T.V.2
  • 13
    • 1342322692 scopus 로고    scopus 로고
    • Conformational changes of β-lactoglobulin in sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles-a fluorescence and CD study
    • Andrade S.M., Cavalho T.I., Viseu M.I., and Costa S.M.B. Conformational changes of β-lactoglobulin in sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles-a fluorescence and CD study. Eur. J. Biochem. 271 (2004) 734-744
    • (2004) Eur. J. Biochem. , vol.271 , pp. 734-744
    • Andrade, S.M.1    Cavalho, T.I.2    Viseu, M.I.3    Costa, S.M.B.4
  • 14
    • 1342293174 scopus 로고    scopus 로고
    • Conformational transitions in β-lactoglobulin induced by cationic amphiphiles: equilibrium studies
    • Viseu M.I., Carvalho T.I., and Costa S.M.B. Conformational transitions in β-lactoglobulin induced by cationic amphiphiles: equilibrium studies. Biophys. J. 86 (2004) 2392-2402
    • (2004) Biophys. J. , vol.86 , pp. 2392-2402
    • Viseu, M.I.1    Carvalho, T.I.2    Costa, S.M.B.3
  • 15
    • 0000378448 scopus 로고
    • Circular dichroism of peptides and proteins
    • Nakanish K., Barova N., and Woody R.W. (Eds), VCH Publishers, Inc., New York
    • Woody R. Circular dichroism of peptides and proteins. In: Nakanish K., Barova N., and Woody R.W. (Eds). Circular Dichroism: Principles and Applications (1994), VCH Publishers, Inc., New York 483-487
    • (1994) Circular Dichroism: Principles and Applications , pp. 483-487
    • Woody, R.1
  • 16
    • 0015997959 scopus 로고
    • Aromatic contributions to circular dichroism spectra of proteins
    • Strickland E.H. Aromatic contributions to circular dichroism spectra of proteins. CRC Crit. Rev. Biochem. 2 (1974) 113-175
    • (1974) CRC Crit. Rev. Biochem. , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 17
    • 0033230053 scopus 로고    scopus 로고
    • Effect of heat treatment on the circular dichroism spectra of bovine beta-lactoglobulin A, B, and C
    • Manderson G.A., Creamer L.K., and Hardman M.J. Effect of heat treatment on the circular dichroism spectra of bovine beta-lactoglobulin A, B, and C. J. Agric. Food Chem. 47 (1999) 4557-4567
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 4557-4567
    • Manderson, G.A.1    Creamer, L.K.2    Hardman, M.J.3
  • 18
    • 0034792064 scopus 로고    scopus 로고
    • Thermal unfolding of monomeric and dimeric β-lactoglobulins
    • Fessas D., Iametti S., Schiraldi A., and Bonomi F. Thermal unfolding of monomeric and dimeric β-lactoglobulins. Eur. J. Biochem. 268 (2001) 5439-5448
    • (2001) Eur. J. Biochem. , vol.268 , pp. 5439-5448
    • Fessas, D.1    Iametti, S.2    Schiraldi, A.3    Bonomi, F.4
  • 19
    • 0028246854 scopus 로고
    • Probing the retinol-binding site of bovine β-lactoglobulin
    • Cho Y., Batt C.A., and Sawyer L. Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem. 269 (1994) 11102-11107
    • (1994) J. Biol. Chem. , vol.269 , pp. 11102-11107
    • Cho, Y.1    Batt, C.A.2    Sawyer, L.3
  • 20
    • 0033804580 scopus 로고    scopus 로고
    • Heat treatment of β-lactoglobulin: structural changes studied by partitioning and fluorescence
    • Palazolo G., Rodriguez F., Farruggia B., Pico G., and Delorenzi N. Heat treatment of β-lactoglobulin: structural changes studied by partitioning and fluorescence. J. Agric. Food Chem. 48 (2000) 3817-3822
    • (2000) J. Agric. Food Chem. , vol.48 , pp. 3817-3822
    • Palazolo, G.1    Rodriguez, F.2    Farruggia, B.3    Pico, G.4    Delorenzi, N.5
  • 21
    • 0001733592 scopus 로고    scopus 로고
    • Interaction between β-lactoglobulin and phospholipids at the air/water interface
    • Bos M.A., and Nylander T. Interaction between β-lactoglobulin and phospholipids at the air/water interface. Langmuir 12 (1996) 2791-2797
    • (1996) Langmuir , vol.12 , pp. 2791-2797
    • Bos, M.A.1    Nylander, T.2
  • 22
    • 0030666662 scopus 로고    scopus 로고
    • Charge-dependent insertion of beta-lactoglobulin into monoglyceride monolayers
    • Leenhouts J.M., Demel R.A., de Kruijff B., and Boots J.W.P. Charge-dependent insertion of beta-lactoglobulin into monoglyceride monolayers. Biochim. Biophys. Acta 1330 (1997) 61-70
    • (1997) Biochim. Biophys. Acta , vol.1330 , pp. 61-70
    • Leenhouts, J.M.1    Demel, R.A.2    de Kruijff, B.3    Boots, J.W.P.4
  • 23
    • 0032794187 scopus 로고    scopus 로고
    • Interaction mode specific reorganization of gel phase monoglyceride bilayers by β-lactoglobulin
    • Boots J.W.P., Chupin V., Killian J.A., Demel R.A., and de Kruijff B. Interaction mode specific reorganization of gel phase monoglyceride bilayers by β-lactoglobulin. Biochim. Biophys. Acta 1420 (1999) 241-251
    • (1999) Biochim. Biophys. Acta , vol.1420 , pp. 241-251
    • Boots, J.W.P.1    Chupin, V.2    Killian, J.A.3    Demel, R.A.4    de Kruijff, B.5
  • 24
    • 85012509317 scopus 로고
    • Studies of the dielectric properties of protein solutions: III. Lactoglobulin
    • Ferry J.D., and Oncley J.L. Studies of the dielectric properties of protein solutions: III. Lactoglobulin. J. Am. Chem. Soc. 63 (1941) 272-278
    • (1941) J. Am. Chem. Soc. , vol.63 , pp. 272-278
    • Ferry, J.D.1    Oncley, J.L.2
  • 25
    • 0024338903 scopus 로고
    • Interaction of staphylococcal δ-toxin and synthetic analogues with erythrocytes and phospholipid vesicles-biological and physical properties of the amphipathic peptides
    • Alouf J.E., Dufourcq J., Thiaudiere E., and Geoffroy C. Interaction of staphylococcal δ-toxin and synthetic analogues with erythrocytes and phospholipid vesicles-biological and physical properties of the amphipathic peptides. Eur. J. Biochem. 183 (1989) 381-390
    • (1989) Eur. J. Biochem. , vol.183 , pp. 381-390
    • Alouf, J.E.1    Dufourcq, J.2    Thiaudiere, E.3    Geoffroy, C.4
  • 26
    • 0019885217 scopus 로고
    • The adsorption of divalent cations to phosphatidylglycerol bilayer membranes
    • Lau A., McLaughlin A., and McLaughlin S. The adsorption of divalent cations to phosphatidylglycerol bilayer membranes. Biochim. Biophys. Acta 645 (1981) 279-292
    • (1981) Biochim. Biophys. Acta , vol.645 , pp. 279-292
    • Lau, A.1    McLaughlin, A.2    McLaughlin, S.3
  • 27
    • 0001755028 scopus 로고
    • Interaction of phospholipids in monolayers with β-lactoglobulin adsorbed from solution
    • Cornell D.G., and Patterson D.L. Interaction of phospholipids in monolayers with β-lactoglobulin adsorbed from solution. J. Agric. Food Chem. 37 (1989) 1455-1459
    • (1989) J. Agric. Food Chem. , vol.37 , pp. 1455-1459
    • Cornell, D.G.1    Patterson, D.L.2
  • 28
    • 0034633725 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with phospholipid bilayers: a molecular level elucidation as revealed by infrared spectroscopy
    • Lefevere T., and Subirade M. Interaction of β-lactoglobulin with phospholipid bilayers: a molecular level elucidation as revealed by infrared spectroscopy. Int. J. Biol. Macromol. 28 (2000) 59-67
    • (2000) Int. J. Biol. Macromol. , vol.28 , pp. 59-67
    • Lefevere, T.1    Subirade, M.2
  • 29
    • 0030897716 scopus 로고    scopus 로고
    • Calorimetric studies of interactions between β-lactoglobulin and phospholipids in solutions
    • Kristensen A., Nylander T., Paulsson M., and Carlsson A. Calorimetric studies of interactions between β-lactoglobulin and phospholipids in solutions. Int. Dairy J. 7 (1997) 87-92
    • (1997) Int. Dairy J. , vol.7 , pp. 87-92
    • Kristensen, A.1    Nylander, T.2    Paulsson, M.3    Carlsson, A.4
  • 30
    • 51249181265 scopus 로고
    • Complex formation in sonicated mixtures of β-Lactoglobulin and phosphatidylcholine
    • Brown E.M., Carroll R.J., Pfeffer P.E., and Sampugna J. Complex formation in sonicated mixtures of β-Lactoglobulin and phosphatidylcholine. Lipids 18 (1983) 111-118
    • (1983) Lipids , vol.18 , pp. 111-118
    • Brown, E.M.1    Carroll, R.J.2    Pfeffer, P.E.3    Sampugna, J.4


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