메뉴 건너뛰기




Volumn 47, Issue 11, 1999, Pages 4557-4567

Effect of heat treatment on the circular dichroism spectra of bovine β- lactoglobulin A, B, and C

Author keywords

lactoglobulin variants; Aggregate formation; Circular dichroism; Disulfide linked aggregates; Thermal denaturation

Indexed keywords

BETA LACTOGLOBULIN; LACTOGLOBULIN;

EID: 0033230053     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf981291m     Document Type: Article
Times cited : (91)

References (69)
  • 2
    • 0014211099 scopus 로고
    • The isolation and properties of bovine β-lactoglobulin C
    • Bell, K.; McKenzie, H. A. The isolation and properties of bovine β-lactoglobulin C. Biochim. Biophys. Acta 1967, 147, 109-122.
    • (1967) Biochim. Biophys. Acta , vol.147 , pp. 109-122
    • Bell, K.1    McKenzie, H.A.2
  • 6
    • 0028989022 scopus 로고
    • Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin
    • Creamer, L. K. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin. Biochemistry 1995, 34, 7170-7176.
    • (1995) Biochemistry , vol.34 , pp. 7170-7176
    • Creamer, L.K.1
  • 7
    • 0001371844 scopus 로고    scopus 로고
    • Relationship between milk protein polymorphism and differences in physicochemical properties
    • International Dairy Federation: Brussels, Belgium
    • Creamer, L. K.; Harris, D. P. Relationship between milk protein polymorphism and differences in physicochemical properties. In International Dairy Federation Special Issue 9702. Milk Protein Polymorphism; International Dairy Federation: Brussels, Belgium, 1997; pp 110-123.
    • (1997) International Dairy Federation Special Issue 9702. Milk Protein Polymorphism , pp. 110-123
    • Creamer, L.K.1    Harris, D.P.2
  • 8
    • 0030041320 scopus 로고    scopus 로고
    • Infrared and circular dichroism spectroscopic characterization of structural differences between β-lactoglobulin A and B
    • Dong, A.; Matsuura, J.; Allison, S. D.; Chrisman, E.; Manning, M. C.; Carpenter, J. F. Infrared and circular dichroism spectroscopic characterization of structural differences between β-lactoglobulin A and B. Biochemistry 1996, 35, 1450-1457.
    • (1996) Biochemistry , vol.35 , pp. 1450-1457
    • Dong, A.1    Matsuura, J.2    Allison, S.D.3    Chrisman, E.4    Manning, M.C.5    Carpenter, J.F.6
  • 10
    • 0030118518 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin studied by dynamic light scattering
    • Elofsson, U. M.; Dejmek, P.; Paulsson, M. A. Heat-induced aggregation of β-lactoglobulin studied by dynamic light scattering. Int. Dairy J. 1996, 6, 343-357.
    • (1996) Int. Dairy J. , vol.6 , pp. 343-357
    • Elofsson, U.M.1    Dejmek, P.2    Paulsson, M.A.3
  • 11
    • 0002521795 scopus 로고    scopus 로고
    • The relationship between milk protein polymorphism and the manufacture and functionality of dairy products
    • International Dairy Federation: Brussels, Belgium
    • FitzGerald, R. J.; Hill, J. P. The relationship between milk protein polymorphism and the manufacture and functionality of dairy products. In International Dairy Federation Special Issue 9702. Milk Protein Polymorphism; International Dairy Federation: Brussels, Belgium, 1997; pp 355-371.
    • (1997) International Dairy Federation Special Issue 9702. Milk Protein Polymorphism , pp. 355-371
    • FitzGerald, R.J.1    Hill, J.P.2
  • 12
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin family: Structure and function
    • Flower, D. R. The lipocalin family: structure and function. Biochem. J. 1996, 318, 1-14.
    • (1996) Biochem. J. , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 14
    • 0027959547 scopus 로고
    • Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II
    • Freskgård, P.-O.; Mårtensson, L.-G.; Jonasson, P.; Jonsson, B.-H.; Carlsson, U. Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II. Biochemistry 1994, 33, 14281-14288.
    • (1994) Biochemistry , vol.33 , pp. 14281-14288
    • Freskgård, P.-O.1    Mårtensson, L.-G.2    Jonasson, P.3    Jonsson, B.-H.4    Carlsson, U.5
  • 15
    • 0001592750 scopus 로고    scopus 로고
    • Heat induced interactions and gelation of mixtures of bovine β-lactoglobulin and α-lactalbumin
    • Gezimati, J.; Creamer, L. K.; Singh, H. Heat induced interactions and gelation of mixtures of bovine β-lactoglobulin and α-lactalbumin. J. Agric. Food Chem. 1997, 45, 1130-1136.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 1130-1136
    • Gezimati, J.1    Creamer, L.K.2    Singh, H.3
  • 16
    • 0028195932 scopus 로고
    • Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins
    • Gimel, J.-C.; Durand, D.; Nicolai, T. Structure and distribution of aggregates formed after heat-induced denaturation of globular proteins. Macromolecules 1994, 27, 583-589.
    • (1994) Macromolecules , vol.27 , pp. 583-589
    • Gimel, J.-C.1    Durand, D.2    Nicolai, T.3
  • 19
    • 0031935279 scopus 로고    scopus 로고
    • Electrophoretic characterization of the protein products formed during heat treatment of whey protein concentrate solutions
    • Havea, P.; Singh, H.; Creamer, L. K.; Campanella, O. H. Electrophoretic characterization of the protein products formed during heat treatment of whey protein concentrate solutions, J. Dairy Res. 1998, 66, 79-91.
    • (1998) J. Dairy Res. , vol.66 , pp. 79-91
    • Havea, P.1    Singh, H.2    Creamer, L.K.3    Campanella, O.H.4
  • 20
    • 1842420747 scopus 로고    scopus 로고
    • Macromolecular interactions in food technology
    • Parris, N., Kato, A., Creamer, L. K., Pearce, R. J., Eds; American Chemical Society: Washington, DC
    • Hill, J. P.; Boland, M. J.; Creamer, L. K.; Anema, S. G.; Otter, D. E.; Paterson, G. R.; Lowe, R.; Motion, R. L.; Thresher, W. C. In Macromolecular Interactions in Food Technology; Parris, N., Kato, A., Creamer, L. K., Pearce, R. J., Eds; ACS Symposium Series 650; American Chemical Society: Washington, DC, 1996; pp 281-294.
    • (1996) ACS Symposium Series , vol.650 , pp. 281-294
    • Hill, J.P.1    Boland, M.J.2    Creamer, L.K.3    Anema, S.G.4    Otter, D.E.5    Paterson, G.R.6    Lowe, R.7    Motion, R.L.8    Thresher, W.C.9
  • 22
    • 0000008542 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds
    • Hoffmann, M. A. M.; van Mil, P. J. J. M. Heat-induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds. J. Agric. Food Chem. 1997, 45, 2942-2948.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 2942-2948
    • Hoffmann, M.A.M.1    Van Mil, P.J.J.M.2
  • 24
    • 0000994885 scopus 로고
    • Relative structural stabilities of β-lactoglobulins A and B as determined by proteolytic susceptibility and differential scanning calorimetry
    • Huang, X-.L.; Catignani, G. L.; Swaisgood, H. E. Relative structural stabilities of β-lactoglobulins A and B as determined by proteolytic susceptibility and differential scanning calorimetry. J. Agric. Food Chem. 1994, 42, 1276-1280.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1276-1280
    • Huang, X.-.L.1    Catignani, G.L.2    Swaisgood, H.E.3
  • 25
    • 0029924648 scopus 로고    scopus 로고
    • Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin
    • Iametti, S.; De Gregori, B.; Vecchio, G.; Bonomi, F. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. Eur. J. Biochem. 1996, 237, 106-112.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 106-112
    • Iametti, S.1    De Gregori, B.2    Vecchio, G.3    Bonomi, F.4
  • 26
    • 0001535102 scopus 로고    scopus 로고
    • Structural features and reversible association of different quarternary structures of β-lactoglobulin
    • Iametti, S.; Scaglioni, L.; Mazzini, S.; Vecchio, G.; Bonomi, F. Structural features and reversible association of different quarternary structures of β-lactoglobulin. J. Agric. Food Chem. 1998, 46, 2159-2166.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 2159-2166
    • Iametti, S.1    Scaglioni, L.2    Mazzini, S.3    Vecchio, G.4    Bonomi, F.5
  • 28
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • Johnson, W. C. Protein secondary structure and circular dichroism: a practical guide. Proteins: Struct., Funct. Genet. 1990, 7, 205-214.
    • (1990) Proteins: Struct., Funct. Genet. , vol.7 , pp. 205-214
    • Johnson, W.C.1
  • 29
    • 0018339835 scopus 로고
    • The interpretation of near-ultraviolet circular dichroism
    • Kahn, P. C. The interpretation of near-ultraviolet circular dichroism. Methods Enzymol. 1979, 61, 339-378.
    • (1979) Methods Enzymol. , vol.61 , pp. 339-378
    • Kahn, P.C.1
  • 30
    • 0030582679 scopus 로고    scopus 로고
    • The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy
    • Kuwajima, K.; Yamaya, H.; Sugai, S. The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. J. Mol. Biol. 1996, 264, 806-822.
    • (1996) J. Mol. Biol. , vol.264 , pp. 806-822
    • Kuwajima, K.1    Yamaya, H.2    Sugai, S.3
  • 31
    • 0032491317 scopus 로고    scopus 로고
    • α → β Transition of β-lactoglobulin as evidenced by heteronuclear NMR
    • Kuwata, K.; Hoshino, M.; Era, S. Batt, C. A.; Goto, Y. α → β Transition of β-lactoglobulin as evidenced by heteronuclear NMR. J. Mol. Biol. 1998, 283, 731-739.
    • (1998) J. Mol. Biol. , vol.283 , pp. 731-739
    • Kuwata, K.1    Hoshino, M.2    Era, S.3    Batt, C.A.4    Goto, Y.5
  • 32
    • 0024460440 scopus 로고
    • Calorimetric and circular dichroic studies of the thermal denaturation of β-lactoglobulin
    • Lapanje, S.; Poklar, G. B. Calorimetric and circular dichroic studies of the thermal denaturation of β-lactoglobulin. Biophys. Chem. 1989, 34, 155-162.
    • (1989) Biophys. Chem. , vol.34 , pp. 155-162
    • Lapanje, S.1    Poklar, G.B.2
  • 34
    • 0029081989 scopus 로고
    • Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dehydrofolate reductase from Escherichia coli
    • Luo, J.; Mathews, C. R.; Iwakura, M. Detection of a stable intermediate in the thermal unfolding of a cysteine-free form of dehydrofolate reductase from Escherichia coli. Biochemistry 1995, 34, 10669-10675.
    • (1995) Biochemistry , vol.34 , pp. 10669-10675
    • Luo, J.1    Mathews, C.2    Iwakura, M.3
  • 36
    • 0344224572 scopus 로고
    • Thermal denaturation of β-lactoglobulin A, B, and C
    • Manderson, G.; Hardman, M. J.; Creamer, L. K. Thermal denaturation of β-lactoglobulin A, B, and C. J. Dairy Sci. 1995, 78 (Suppl. 1), 132.
    • (1995) J. Dairy Sci. , vol.78 , Issue.1 SUPPL. , pp. 132
    • Manderson, G.1    Hardman, M.J.2    Creamer, L.K.3
  • 38
    • 0001205312 scopus 로고    scopus 로고
    • Effect of heat treatment on conformation and aggregation of β-lactoglobulin A, B, and C
    • Manderson, G. A.; Hardman, M. J.; Creamer, L. K. Effect of heat treatment on conformation and aggregation of β-lactoglobulin A, B, and C. J. Agric. Food Chem. 1998, 46, 5052-5061.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 5052-5061
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 39
    • 24544447317 scopus 로고
    • Heat-induced gel formation of β-lactoglobulin: A study on the secondary and tertiary structure as followed by circular dichroism spectroscopy
    • Matsuura, J. E.; Manning, M. C. Heat-induced gel formation of β-lactoglobulin: A study on the secondary and tertiary structure as followed by circular dichroism spectroscopy. J. Agric. Food Chem. 1994, 42, 1650-1656.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1650-1656
    • Matsuura, J.E.1    Manning, M.C.2
  • 40
    • 0000125782 scopus 로고
    • β-Lactoglobulins
    • McKenzie, H. A., Ed.; Academic Press: New York
    • McKenzie, H. A. β-Lactoglobulins. In Milk Proteins. Chemistry and Molecular Biology; McKenzie, H. A., Ed.; Academic Press: New York, 1971; Vol. II, pp 257-330.
    • (1971) Milk Proteins. Chemistry and Molecular Biology , vol.2 , pp. 257-330
    • McKenzie, H.A.1
  • 41
    • 85025345712 scopus 로고
    • Thermal aggregation and gelation of bovine β-lactoglobulin
    • McSwiney, M.; Singh, H.; Campanella, O. Thermal aggregation and gelation of bovine β-lactoglobulin. Food Hydrocolloids 1994a, 8, 441-453.
    • (1994) Food Hydrocolloids , vol.8 , pp. 441-453
    • McSwiney, M.1    Singh, H.2    Campanella, O.3
  • 42
    • 0028087108 scopus 로고
    • Thermal gelation and denaturation of bovine β-lactoglobulins A and B
    • McSwiney, M.; Singh, H.; Campanella, O.; Creamer, L. K. Thermal gelation and denaturation of bovine β-lactoglobulins A and B. J. Dairy Res. 1994b, 61, 221-232.
    • (1994) J. Dairy Res. , vol.61 , pp. 221-232
    • McSwiney, M.1    Singh, H.2    Campanella, O.3    Creamer, L.K.4
  • 43
    • 0017073111 scopus 로고
    • Effect of temperature on tryptophan fluorescence of β-lactoglobulin B
    • Mills, O. E. Effect of temperature on tryptophan fluorescence of β-lactoglobulin B. Biochim. Biophys. Acta 1976, 434, 324-332.
    • (1976) Biochim. Biophys. Acta , vol.434 , pp. 324-332
    • Mills, O.E.1
  • 45
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine β-lactoglobulin and its complex with retinol at 2.5 Å resolution
    • Monaco, H. L.; Zanotti, G.; Spadon, P.; Bolognesi, M.; Sawyer, L.; Eliopoulis, E. E. Crystal structure of the trigonal form of bovine β-lactoglobulin and its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 1987, 197, 695-706.
    • (1987) J. Mol. Biol. , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, M.4    Sawyer, L.5    Eliopoulis, E.E.6
  • 47
    • 0031577271 scopus 로고    scopus 로고
    • Nonenzymatic lactosylation of bovine β-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms
    • Morgan, F.; Léonil, J.; Mollé, D.; Bouhallab, S. Nonenzymatic lactosylation of bovine β-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem. Biophys. Res. Commun. 1997, 236, 413-417.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 413-417
    • Morgan, F.1    Léonil, J.2    Mollé, D.3    Bouhallab, S.4
  • 48
    • 0345059266 scopus 로고    scopus 로고
    • Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: Effect on association behavior and protein conformation
    • Morgan, F.; Léonil, J.; Mollé, D.; Bouhallab, S. Modification of bovine β-lactoglobulin by glycation in a powdered state or in an aqueous solution: effect on association behavior and protein conformation. J. Agric. Food Chem. 1999, 47, 83-91.
    • (1999) J. Agric. Food Chem. , vol.47 , pp. 83-91
    • Morgan, F.1    Léonil, J.2    Mollé, D.3    Bouhallab, S.4
  • 49
    • 0000923426 scopus 로고
    • Genetic polymorphism of milk proteins
    • Fox, P. F., Ed.; Elsevier Applied Science: London, U.K.
    • Ng-Kwai-Hang, K. F.; Grosclaude, F. Genetic polymorphism of milk proteins. In Advanced Dairy Chemistry - 1 Proteins; Fox, P. F., Ed.; Elsevier Applied Science: London, U.K., 1992; pp 405-455.
    • (1992) Advanced Dairy Chemistry - 1 Proteins , pp. 405-455
    • Ng-Kwai-Hang, K.F.1    Grosclaude, F.2
  • 51
    • 0000008540 scopus 로고    scopus 로고
    • Thermal unfolding of β-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation
    • Prabakaran, S.; Damodaran, S. Thermal unfolding of β-lactoglobulin: characterization of initial unfolding events responsible for heat-induced aggregation. J. Agric. Food Chem. 1997, 45, 4303-4308.
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4303-4308
    • Prabakaran, S.1    Damodaran, S.2
  • 52
    • 0028985708 scopus 로고
    • Thermal denaturation of β-lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05
    • Qi, X. L.; Brownlow, S.; Holt, C.; Sellers, P. Thermal denaturation of β-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05. Biochim. Biophys. Acta 1995, 1248, 43-49.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 43-49
    • Qi, X.L.1    Brownlow, S.2    Holt, C.3    Sellers, P.4
  • 53
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • Qi, X. L.; Holt, C.; McNulty, D.; Clarke, D. T.; Brownlow, S.; Jones, G. R. Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochem. J. 1997, 324, 341-346.
    • (1997) Biochem. J. , vol.324 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 54
    • 0031738305 scopus 로고    scopus 로고
    • 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin
    • Qin, B. Y.; Creamer, L. K.; Baker, E. N.; Jameson, G. B. 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Lett. 1998a, 438, 272-278.
    • (1998) FEBS Lett. , vol.438 , pp. 272-278
    • Qin, B.Y.1    Creamer, L.K.2    Baker, E.N.3    Jameson, G.B.4
  • 56
    • 0344656023 scopus 로고    scopus 로고
    • Structural and functional differences of variants A and B of bovine β-lactoglobulin
    • Qin, B. Y.; Bewley, M. C.; Creamer, L. K.; Baker, E. N.; Jameson, G. B. Structural and functional differences of variants A and B of bovine β-lactoglobulin. Protein Sci. 1999, 8, 1-9.
    • (1999) Protein Sci. , vol.8 , pp. 1-9
    • Qin, B.Y.1    Bewley, M.C.2    Creamer, L.K.3    Baker, E.N.4    Jameson, G.B.5
  • 57
    • 0030635208 scopus 로고    scopus 로고
    • Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2
    • Ragona, L.; Pusterla, F.; Zetta, L.; Monaco, H. L.; Molinari, H. Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2. Folding Design 1997, 2, 281-290.
    • (1997) Folding Design , vol.2 , pp. 281-290
    • Ragona, L.1    Pusterla, F.2    Zetta, L.3    Monaco, H.L.4    Molinari, H.5
  • 58
    • 0028567981 scopus 로고
    • A model for the denaturation and aggregation of β-lactoglobulin
    • Roefs, S. P. F. M.; de Kruif, K. G. A model for the denaturation and aggregation of β-lactoglobulin. Eur. J. Biochem. 1994, 226, 883-889.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    De Kruif, K.G.2
  • 59
    • 84976113450 scopus 로고
    • A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate
    • Rüegg, M.; Moor, U.; Blanc, B. A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate. J. Dairy Res. 1977, 44, 509-520.
    • (1977) J. Dairy Res. , vol.44 , pp. 509-520
    • Rüegg, M.1    Moor, U.2    Blanc, B.3
  • 60
    • 0015239798 scopus 로고
    • Thermodenaturation of bovine β-lactoglobulin kinetics and introduction of β-structure
    • Sawyer, W. H.; Norton, R. S.; Nichol, L. W.; McKenzie, G. H. Thermodenaturation of bovine β-lactoglobulin kinetics and introduction of β-structure. Biochim. Biophys. Acta 1971, 243, 19-30.
    • (1971) Biochim. Biophys. Acta , vol.243 , pp. 19-30
    • Sawyer, W.H.1    Norton, R.S.2    Nichol, L.W.3    McKenzie, G.H.4
  • 61
    • 0015997959 scopus 로고
    • Aromatic contribution to circular dichroism spectra of proteins
    • Strickland, E. H. Aromatic contribution to circular dichroism spectra of proteins. CRC Crit. Rev. Biochem. 1974, 2, 113-175.
    • (1974) CRC Crit. Rev. Biochem. , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 62
    • 0014010739 scopus 로고
    • Conformational transitions of bovine β-lactoglobulins A, B, and C
    • Timasheff, S. N.; Mescanti, L.; Basch, J. J.; Townend, R. Conformational transitions of bovine β-lactoglobulins A, B, and C. J. Biol. Chem. 1966, 241, 2496-2501.
    • (1966) J. Biol. Chem. , vol.241 , pp. 2496-2501
    • Timasheff, S.N.1    Mescanti, L.2    Basch, J.J.3    Townend, R.4
  • 63
    • 0010971688 scopus 로고
    • Application of circular dichroism and infrared spectroscopy to the conformation of proteins in solution
    • Ramachandran, G. N., Ed.; Academic Press: New York
    • Timasheff, S. N.; Susi, H.; Townend, R.; Stevens, L.; Gorbunoff, M. J.; Kumosinski, T. F. Application of circular dichroism and infrared spectroscopy to the conformation of proteins in solution. In Conformation of Biopolymers; Ramachandran, G. N., Ed.; Academic Press: New York, 1967; Vol. 1, pp 173-196.
    • (1967) Conformation of Biopolymers , vol.1 , pp. 173-196
    • Timasheff, S.N.1    Susi, H.2    Townend, R.3    Stevens, L.4    Gorbunoff, M.J.5    Kumosinski, T.F.6
  • 64
    • 0014199124 scopus 로고
    • The circular dichroism of variants of β-lactoglobulin
    • Townend, R.; Kumosinski, T. F.; Timasheff, S. N. The circular dichroism of variants of β-lactoglobulin. J. Biol. Chem. 1967, 242, 4538-4545.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4538-4545
    • Townend, R.1    Kumosinski, T.F.2    Timasheff, S.N.3
  • 65
    • 0032110129 scopus 로고    scopus 로고
    • 15N chemical shifts for bovine β-lactoglobulin - Secondary structure and topology of the native state is retained in a partially unfolded form
    • 15N chemical shifts for bovine β-lactoglobulin - secondary structure and topology of the native state is retained in a partially unfolded form. J. Biomol. NMR 1998, 12, 89-107.
    • (1998) J. Biomol. NMR , vol.12 , pp. 89-107
    • Uhrínová, S.1    Uhrín, D.2    Denton, H.3    Smith, M.4    Sawyer, L.5    Barlow, P.N.6
  • 66
  • 67
    • 0001765072 scopus 로고
    • Application of the bergson model to the optical properties of chiral disulfides
    • Woody, R. W. Application of the Bergson model to the optical properties of chiral disulfides. Tetrahedron 1973, 1273-1283.
    • (1973) Tetrahedron , pp. 1273-1283
    • Woody, R.W.1
  • 68
    • 0028959773 scopus 로고
    • Circular dichroism
    • Woody, R. W. Circular dichroism. Methods Enzymol. 1995, 246, 34-71.
    • (1995) Methods Enzymol. , vol.246 , pp. 34-71
    • Woody, R.W.1
  • 69
    • 0345313659 scopus 로고    scopus 로고
    • β-Lactoglobulin binds palmitate within its central cavity
    • Wu, S. Y.; Pérez, M. D.; Puyol, P.; Sawyer, L. β-Lactoglobulin binds palmitate within its central cavity. J. Biol. Chem. 1999, 274, 170-174.
    • (1999) J. Biol. Chem. , vol.274 , pp. 170-174
    • Wu, S.Y.1    Pérez, M.D.2    Puyol, P.3    Sawyer, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.