-
1
-
-
0026530383
-
Quantitative analysis of protein far UV circular dishroism spectra by neural networks
-
Bohm, G., Muhr, R., and Jaenicke, R. 1992. Quantitative analysis of protein far UV circular dishroism spectra by neural networks. Protein Eng. 5: 191-195.
-
(1992)
Protein Eng.
, vol.5
, pp. 191-195
-
-
Bohm, G.1
Muhr, R.2
Jaenicke, R.3
-
2
-
-
0004907667
-
Bovine β-lactoglobulin at 1.8 Ångstrom resolution - Still an enigmatic lipocalin
-
Brownlow, S., Cabral, J.H.M., Cooper, R., Flower, D.R., Yewdall, S.J., Polikaropov, I., North, A.C.T., and Sawyer, L. 1997. Bovine β -lactoglobulin at 1.8 Ångstrom resolution - still an enigmatic lipocalin. Structure 5: 481-495.
-
(1997)
Structure
, vol.5
, pp. 481-495
-
-
Brownlow, S.1
Cabral, J.H.M.2
Cooper, R.3
Flower, D.R.4
Yewdall, S.J.5
Polikaropov, I.6
North, A.C.T.7
Sawyer, L.8
-
3
-
-
0036403888
-
Use of fluorescence methods to monitor unfolding transitions in β-lactoglobulin
-
Busti, P., Scarpeci, S., Gatti, C., and Delorenzi, N. 2002. Use of fluorescence methods to monitor unfolding transitions in β-lactoglobulin. Food Res. Int. 35: 871-877.
-
(2002)
Food Res. Int.
, vol.35
, pp. 871-877
-
-
Busti, P.1
Scarpeci, S.2
Gatti, C.3
Delorenzi, N.4
-
4
-
-
0002118011
-
The molten globule state of protein molecule is becoming the rule rather than the exception
-
Bychkova, V.Y. and Ptitsyn, O.B. 1993. The molten globule state of protein molecule is becoming the rule rather than the exception. Biophysics 38: 51-58.
-
(1993)
Biophysics
, vol.38
, pp. 51-58
-
-
Bychkova, V.Y.1
Ptitsyn, O.B.2
-
5
-
-
0034967751
-
Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation
-
Carrotta, R., Bauer, R., Waninge, R., and Rischel, C. 2001. Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation. Protein Sci. 10: 1312-1318.
-
(2001)
Protein Sci.
, vol.10
, pp. 1312-1318
-
-
Carrotta, R.1
Bauer, R.2
Waninge, R.3
Rischel, C.4
-
6
-
-
0032516433
-
Towards understanding tryptophan fluorescence in proteins
-
Chen, Y. and Barkley, M.D. 1998. Towards understanding tryptophan fluorescence in proteins. Biochemistry 37: 9976-9982.
-
(1998)
Biochemistry
, vol.37
, pp. 9976-9982
-
-
Chen, Y.1
Barkley, M.D.2
-
7
-
-
0028246854
-
Probing the retinol-binding site of bovine β-lactoglobulin
-
Cho, Y., Batt, C.A., and Sawyer, L. 1994. Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem. 269: 11102-11107.
-
(1994)
J. Biol. Chem.
, vol.269
, pp. 11102-11107
-
-
Cho, Y.1
Batt, C.A.2
Sawyer, L.3
-
8
-
-
0031026007
-
How important is the molten globule for correct protein folding?
-
Creighton, T.E. 1997. How important is the molten globule for correct protein folding? Trends Biochem. Sci. 22: 6-10.
-
(1997)
Trends Biochem. Sci.
, vol.22
, pp. 6-10
-
-
Creighton, T.E.1
-
9
-
-
0037423721
-
Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin
-
Croguennec, T., Bouhallab, S., Molle, D., O'Kennedy, B.T., and Mehra, R. 2003. Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin. Biochem. Biophys. Res. Com. 301: 465-471.
-
(2003)
Biochem. Biophys. Res. Com.
, vol.301
, pp. 465-471
-
-
Croguennec, T.1
Bouhallab, S.2
Molle, D.3
O'Kennedy, B.T.4
Mehra, R.5
-
10
-
-
1542575976
-
Heat-induced denaturation/aggregation of β-lactoglobulin A and B: Kinetics of the first intermediates formed
-
in press
-
Croguennec, T., O'Kennedy, B.T., and Mehra, R. 2004. Heat-induced denaturation/aggregation of β-lactoglobulin A and B: Kinetics of the first intermediates formed. Int. Dairy J. (in press).
-
(2004)
Int. Dairy J.
-
-
Croguennec, T.1
O'Kennedy, B.T.2
Mehra, R.3
-
11
-
-
0036704306
-
Recent advances in the characterization of heat-induced aggregates and intermediates of whey proteins
-
De la Fuente, M.A., Singh, H., and Hemar, Y. 2002. Recent advances in the characterization of heat-induced aggregates and intermediates of whey proteins. Trends Food Sci. Technol. 13: 262-274.
-
(2002)
Trends Food Sci. Technol.
, vol.13
, pp. 262-274
-
-
De La Fuente, M.A.1
Singh, H.2
Hemar, Y.3
-
12
-
-
0025847935
-
The molten globule protein conformation probed by disulfide bonds
-
Ewbank, J.J. and Creighton, T.E. 1991. The molten globule protein conformation probed by disulfide bonds. Nature 350: 518-520.
-
(1991)
Nature
, vol.350
, pp. 518-520
-
-
Ewbank, J.J.1
Creighton, T.E.2
-
13
-
-
0034792064
-
Thermal unfolding of monomeric and dimeric β-lactoglobulins
-
Fessas, D., Iametti, S., Schiraldi, A., and Bonomi, F. 2001. Thermal unfolding of monomeric and dimeric β-lactoglobulins. Eur. J. Biochem. 268: 5439-5448.
-
(2001)
Eur. J. Biochem.
, vol.268
, pp. 5439-5448
-
-
Fessas, D.1
Iametti, S.2
Schiraldi, A.3
Bonomi, F.4
-
14
-
-
0030982174
-
Quenching of tryptophan fluorescence by the active-site disulfide bridge in the DsbA protein from Escherichia coli
-
Hennecke, J., Sillen, A., Huber-Wunderlich, M., Engelborghs, Y., and Glockohuber, R. 1997. Quenching of tryptophan fluorescence by the active-site disulfide bridge in the DsbA protein from Escherichia coli. Biochemistry 36: 6391-6400.
-
(1997)
Biochemistry
, vol.36
, pp. 6391-6400
-
-
Hennecke, J.1
Sillen, A.2
Huber-Wunderlich, M.3
Engelborghs, Y.4
Glockohuber, R.5
-
15
-
-
0000266449
-
Interactions of α-lactalbumin and bovine serum albumin with β-lactoglobulin in thermally induced gelation
-
Hines, M.E. and Foegeding, E.A. 1993. Interactions of α-lactalbumin and bovine serum albumin with β-lactoglobulin in thermally induced gelation. J. Agric. Food Chem. 41: 341-346.
-
(1993)
J. Agric. Food Chem.
, vol.41
, pp. 341-346
-
-
Hines, M.E.1
Foegeding, E.A.2
-
16
-
-
0027543524
-
Molten globule state of food proteins
-
Hirose, M. 1993. Molten globule state of food proteins. Trends Food Sci. Technol. 4: 48-51.
-
(1993)
Trends Food Sci. Technol.
, vol.4
, pp. 48-51
-
-
Hirose, M.1
-
17
-
-
0000008542
-
Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds
-
Hoffmann, M.A.M. and Van Mil, P.J.J.M. 1997. Heat-induced aggregation of β-lactoglobulin: Role of the free thiol group and disulfide bonds. J. Agric. Food Chem. 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
-
18
-
-
0347923607
-
Heat-induced aggregation behavior of bovine β-lactoglobulin B
-
Hong, Y.H. and Creamer, L.K. 2002. Heat-induced aggregation behavior of bovine β-lactoglobulin B. Food Sci. Biotechnol. 11: 161-164.
-
(2002)
Food Sci. Biotechnol.
, vol.11
, pp. 161-164
-
-
Hong, Y.H.1
Creamer, L.K.2
-
19
-
-
0029924648
-
Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin
-
Iametti, S., Degregori, B., Vecchio, G., and Bonomi, F. 1996. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. Eur. J. Biochem. 237: 106-112.
-
(1996)
Eur. J. Biochem.
, vol.237
, pp. 106-112
-
-
Iametti, S.1
Degregori, B.2
Vecchio, G.3
Bonomi, F.4
-
20
-
-
0034850884
-
Pressure-induced denaturation of monomer β-lactoglobulin is partially irreversible: Comparison of monomer form (highly acidic pH) with dimer from (neutral pH)
-
Ikeuchi, Y., Nakagawa, K., Endo, T., Suzuki, A., Hayashi, T., and Ito, T. 2001. Pressure-induced denaturation of monomer β-lactoglobulin is partially irreversible: Comparison of monomer form (highly acidic pH) with dimer from (neutral pH). J. Agric. Food Chem. 49: 4052-4059.
-
(2001)
J. Agric. Food Chem.
, vol.49
, pp. 4052-4059
-
-
Ikeuchi, Y.1
Nakagawa, K.2
Endo, T.3
Suzuki, A.4
Hayashi, T.5
Ito, T.6
-
21
-
-
0002593957
-
Calcium binding and salt-induced structural changes of native and preheated β-lactoglobulin
-
Jeyarajah, S. and Allen, J.C. 1994. Calcium binding and salt-induced structural changes of native and preheated β-lactoglobulin. J. Agric. Food Chem. 42: 80-85.
-
(1994)
J. Agric. Food Chem.
, vol.42
, pp. 80-85
-
-
Jeyarajah, S.1
Allen, J.C.2
-
22
-
-
0034856440
-
Reversible conformational change in β-lactoglobulin modified with N-ethylmaleimide and resistance to molecular aggregation on heating
-
Kitabatake, N., Wada, R., and Fujita, Y. 2001. Reversible conformational change in β-lactoglobulin modified with N-ethylmaleimide and resistance to molecular aggregation on heating. J. Agric. Food Chem. 49: 4011-4018.
-
(2001)
J. Agric. Food Chem.
, vol.49
, pp. 4011-4018
-
-
Kitabatake, N.1
Wada, R.2
Fujita, Y.3
-
23
-
-
0036037132
-
The ligand-binding site of bovine β-lactoglobulin: Evidence for a function?
-
Kontopidis, G., Holt, G., and Sawyer, L. 2002. The ligand-binding site of bovine β-lactoglobulin: Evidence for a function? J. Mol. Biol. 318: 1043-1055.
-
(2002)
J. Mol. Biol.
, vol.318
, pp. 1043-1055
-
-
Kontopidis, G.1
Holt, G.2
Sawyer, L.3
-
24
-
-
0031999033
-
Large scale preparation of β-lactoglobulin A and B by ultrafiltration and ion-exchange chromatography
-
Kristiansen, K.R., Otte, J., Ipsen, R., and Qvist, K.B. 1998. Large scale preparation of β-lactoglobulin A and B by ultrafiltration and ion-exchange chromatography. Int. Dairy J. 8: 113-118.
-
(1998)
Int. Dairy J.
, vol.8
, pp. 113-118
-
-
Kristiansen, K.R.1
Otte, J.2
Ipsen, R.3
Qvist, K.B.4
-
25
-
-
0030582679
-
The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy
-
Kuwajima, K., Yamaya, H., and Sugai, S. 1996. The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy. J. Mol. Biol. 264: 806-822.
-
(1996)
J. Mol. Biol.
, vol.264
, pp. 806-822
-
-
Kuwajima, K.1
Yamaya, H.2
Sugai, S.3
-
26
-
-
0001205312
-
Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A
-
Manderson, G.A., Hardman, M.J., and Creamer, L.K. 1998. Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B, and C. J. Agric. Food Chem. 46: 5052-5061.
-
(1998)
B, and C. J. Agric. Food Chem.
, vol.46
, pp. 5052-5061
-
-
Manderson, G.A.1
Hardman, M.J.2
Creamer, L.K.3
-
27
-
-
0032839589
-
Effect of heat treatment on bovine β-lactoglobulin A, B, and C explored using thiol availability and fluorescence
-
-. 1999. Effect of heat treatment on bovine β-lactoglobulin A, B, and C explored using thiol availability and fluorescence. J. Agric. Food Chem. 47: 3617-3627.
-
(1999)
J. Agric. Food Chem.
, vol.47
, pp. 3617-3627
-
-
-
28
-
-
24544447317
-
Heat-induced gel formation of β-lactoglobulin: A study on the secondary and tertiary structure as followed by circular dichroism spectroscopy
-
Matsuura, J.E. and Manning, M.C. 1994. 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. 42: 1650-1656.
-
(1994)
J. Agric. Food Chem.
, vol.42
, pp. 1650-1656
-
-
Matsuura, J.E.1
Manning, M.C.2
-
29
-
-
0016662215
-
Conformational change in bovine β-lactoglobulin at low pH
-
Mills, O.E. and Creamer, L.K.A. 1975. Conformational change in bovine β-lactoglobulin at low pH. Biochem. Biophys. Acta 379: 618-626.
-
(1975)
Biochem. Biophys. Acta
, vol.379
, pp. 618-626
-
-
Mills, O.E.1
Creamer, L.K.A.2
-
30
-
-
0022931198
-
The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein
-
Papiz, M.Z., Sawyer, L., Eliopoulos, E.E., North, A.C.T., Findlay, J.B.C., Sivaprasadarao, R., Jones, T.A., Newcomer, M.E., and Kraulis, P.J. 1986. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324: 383-385.
-
(1986)
Nature
, vol.324
, pp. 383-385
-
-
Papiz, M.Z.1
Sawyer, L.2
Eliopoulos, E.E.3
North, A.C.T.4
Findlay, J.B.C.5
Sivaprasadarao, R.6
Jones, T.A.7
Newcomer, M.E.8
Kraulis, P.J.9
-
31
-
-
0000008540
-
Thermal unfolding of β-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation
-
Prabakaran, S. and Damodaran, S. 1997. Thermal unfolding of β-lactoglobulin: Characterization of initial unfolding events responsible for heat-induced aggregation. J. Agric. Food Chem. 45: 4303-4308.
-
(1997)
J. Agric. Food Chem.
, vol.45
, pp. 4303-4308
-
-
Prabakaran, S.1
Damodaran, S.2
-
32
-
-
0030993642
-
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., and Jones, G.R. 1997. 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. 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
-
33
-
-
0032004945
-
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. 1998. Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies. Int. J. Biol. Macromol. 22: 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
-
34
-
-
0034684161
-
The core lipocalin, bovine β-lactoglobulin
-
Sawyer, L. and Kontopidis, G. 2000. The core lipocalin, bovine β-lactoglobulin. Biochem. Biophys. Acta 1482: 136-148.
-
(2000)
Biochem. Biophys. Acta
, vol.1482
, pp. 136-148
-
-
Sawyer, L.1
Kontopidis, G.2
-
35
-
-
0033501546
-
Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH
-
Schokker, E.P., Singh, H., Pinder, D.N., Norris, G.E., and Creamer, L.K. 1999. Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH. Int. Dairy J. 9: 791-800.
-
(1999)
Int. Dairy J.
, vol.9
, pp. 791-800
-
-
Schokker, E.P.1
Singh, H.2
Pinder, D.N.3
Norris, G.E.4
Creamer, L.K.5
-
36
-
-
0029936006
-
Modification of the single unpaired sulfhydryl group of β-lactoglobulin under high pressure and the role of intermolecular S-S exchange in the pressure denaturation [Single SH of β-lactoglobulin and pressure denaturation]
-
Tanaka, N., Tsurui, Y., Kobayashi, I., and Kunugi, S. 1996. Modification of the single unpaired sulfhydryl group of β-lactoglobulin under high pressure and the role of intermolecular S-S exchange in the pressure denaturation [Single SH of β-lactoglobulin and pressure denaturation]. Int. J. Biol. Macromol. 19: 63-68.
-
(1996)
Int. J. Biol. Macromol.
, vol.19
, pp. 63-68
-
-
Tanaka, N.1
Tsurui, Y.2
Kobayashi, I.3
Kunugi, S.4
-
37
-
-
0001497241
-
The reversible transformation of β-lactoglobulin at pH 7.5
-
Tanford, C., Bunville, L.G., and Nozaki, Y. 1959. The reversible transformation of β-lactoglobulin at pH 7.5. J. Am. Chem. Soc. 81: 4032-4036.
-
(1959)
J. Am. Chem. Soc.
, vol.81
, pp. 4032-4036
-
-
Tanford, C.1
Bunville, L.G.2
Nozaki, Y.3
|