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Volumn 39, Issue 4, 2000, Pages 317-330

Electrostatic properties of bovine β-Lactoglobulin

Author keywords

Continuum methods; Electrostatic forces; NMR; Poisson Boltzmann; Protein titration

Indexed keywords

BETA LACTOGLOBULIN;

EID: 0034214419     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000601)39:4<317::AID-PROT50>3.0.CO;2-W     Document Type: Article
Times cited : (79)

References (46)
  • 3
    • 0032923417 scopus 로고    scopus 로고
    • Functional implications of structural differences between variants A and B of bovine β-lactoglobulin
    • Qin BY, Bewley MC, Creamer LK, Baker EN, Jameson GB. Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Protein Sci 1999;8:75-83
    • (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
  • 5
    • 0030635208 scopus 로고    scopus 로고
    • Identification of a conserved hydrophobic cluster in partially folded β-lactoglobulin at pH 2
    • Ragona L, Pusterla F, Zetta L, Monaco HL, Molinari H. Identification of a conserved hydrophobic cluster in partially folded β-lactoglobulin at pH 2. Fold Des 1997;2:281-290.
    • (1997) Fold Des , vol.2 , pp. 281-290
    • Ragona, L.1    Pusterla, F.2    Zetta, L.3    Monaco, H.L.4    Molinari, H.5
  • 7
    • 0032110129 scopus 로고    scopus 로고
    • Complete assignment of 1H, 13C and 15N chemical shifts for bovine β-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, Barlow PN, Complete assignment of 1H, 13C and 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
    • Uhrinova, S.1    Uhrin, D.2    Denton, H.3    Smith, M.4    Sawyer, L.5    Barlow, P.N.6
  • 8
    • 0033527582 scopus 로고    scopus 로고
    • Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements
    • Ragona L, Fogolari F, Romagnoli S, Zetta L, Maubois JL, Molinari H. Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements. J Mol Biol 1999;293:953-969.
    • (1999) J Mol Biol , vol.293 , pp. 953-969
    • Ragona, L.1    Fogolari, F.2    Romagnoli, S.3    Zetta, L.4    Maubois, J.L.5    Molinari, H.6
  • 9
    • 0032483094 scopus 로고    scopus 로고
    • Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: A method of binding site determination using fluorescence resonance energy transfer
    • Lange DC, Kothari R, Patel RC, Patel SC. Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: a method of binding site determination using fluorescence resonance energy transfer. Biophys Chem 1998;74:45-51.
    • (1998) Biophys Chem , vol.74 , pp. 45-51
    • Lange, D.C.1    Kothari, R.2    Patel, R.C.3    Patel, S.C.4
  • 10
    • 0027549546 scopus 로고
    • Comparison of the ability to bind lipids of β-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species
    • Perez DM, Pujol P, Ena JM, Calvo M. Comparison of the ability to bind lipids of β-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species. J Dairy Res 1993;60:55-63.
    • (1993) J Dairy Res , vol.60 , pp. 55-63
    • Perez, D.M.1    Pujol, P.2    Ena, J.M.3    Calvo, M.4
  • 11
    • 0345313659 scopus 로고    scopus 로고
    • β-lactoglobulin binds palmitate within its central cavity
    • Wu S, Perez DM, 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.1    Perez, D.M.2    Puyol, P.3    Sawyer, L.4
  • 12
    • 4243463817 scopus 로고
    • Electrostatics in biomolecular structure and dynamics
    • Davis ME, McCammon JA. Electrostatics in biomolecular structure and dynamics, Chem Rev 1990;90:509-521.
    • (1990) Chem Rev , vol.90 , pp. 509-521
    • Davis, M.E.1    McCammon, J.A.2
  • 13
    • 0029016182 scopus 로고
    • Classical electrostatic in biology and chemistry
    • Honig B, Nicholls A. Classical electrostatic in biology and chemistry, Science 1995;268:1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 14
    • 85050521214 scopus 로고
    • Biological applications of electrostatics calculations and Brownian dynamics simulations
    • 1994
    • Madura JD, Davis ME, Gilson MK, Wade R, Luty BA, McCammon JA (1994). Biological applications of electrostatics calculations and Brownian dynamics simulations, Rev Comp Chem 1994;5:229-267.
    • (1994) Rev Comp Chem , vol.5 , pp. 229-267
    • Madura, J.D.1    Davis, M.E.2    Gilson, M.K.3    Wade, R.4    Luty, B.A.5    McCammon, J.A.6
  • 16
    • 0032937077 scopus 로고    scopus 로고
    • Biomolecular electrostatics with the linearized Poisson-Boltzmann equation
    • Fogolari F, Zuccato P, Esposito G, Viglino P. Biomolecular electrostatics with the linearized Poisson-Boltzmann equation. Biophys J 1999;76:1-16.
    • (1999) Biophys J , vol.76 , pp. 1-16
    • Fogolari, F.1    Zuccato, P.2    Esposito, G.3    Viglino, P.4
  • 17
    • 0020475509 scopus 로고
    • Calculation of the electric potential in the active site cleft due to alpha-helix dipoles
    • Warwicker J, Watson HC. Calculation of the electric potential in the active site cleft due to alpha-helix dipoles. J Mol Biol 1982;157: 671-9.
    • (1982) J Mol Biol , vol.157 , pp. 671-679
    • Warwicker, J.1    Watson, H.C.2
  • 18
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution: Method and error assessment
    • Gilson MK, Sharp KA, Honig B. Calculating the electrostatic potential of molecules in solution: method and error assessment. J Comp Chem 1987;9:327-335.
    • (1987) J Comp Chem , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.3
  • 19
    • 84986532558 scopus 로고
    • Electrostatics energy calculations by a finite-difference method rapid calculations of charge-solvent interaction energies
    • Luty BA, Davis ME, McCammon JA. Electrostatics energy calculations by a finite-difference method rapid calculations of charge-solvent interaction energies. J Comp Chem 1992;13:768-771.
    • (1992) J Comp Chem , vol.13 , pp. 768-771
    • Luty, B.A.1    Davis, M.E.2    McCammon, J.A.3
  • 20
    • 0031547966 scopus 로고    scopus 로고
    • Electrostatic complementarity at protein/protein interfaces
    • McCoy AJ, Chandana Epa V, Colman PM. Electrostatic complementarity at protein/protein interfaces. J Mol Biol 1997;268: 570-84.
    • (1997) J Mol Biol , vol.268 , pp. 570-584
    • McCoy, A.J.1    Chandana Epa, V.2    Colman, P.M.3
  • 22
    • 51149205529 scopus 로고
    • Calculation of thermodynamic properties of polyelectrolytes
    • Marcus, R. A. Calculation of thermodynamic properties of polyelectrolytes. J Chem Phys 1955;23:1057-1068.
    • (1955) J Chem Phys , vol.23 , pp. 1057-1068
    • Marcus, R.A.1
  • 23
    • 0000281387 scopus 로고
    • Macromolecular electrostatics energy within the nonlinear Poisson-Boltzmann equation
    • Zhou H-X. Macromolecular electrostatics energy within the nonlinear Poisson-Boltzmann equation. J Chem Phys 1994; 100:3152-3162.
    • (1994) J Chem Phys , vol.100 , pp. 3152-3162
    • Zhou, H.-X.1
  • 24
    • 33751552991 scopus 로고
    • Calculating total electrostatic energies with the non-linear Poisson-Boltzmann equation
    • Sharp KA, Honig B. Calculating total electrostatic energies with the non-linear Poisson-Boltzmann equation, J Phys Chem 1990;94: 7684-7692.
    • (1990) J Phys Chem , vol.94 , pp. 7684-7692
    • Sharp, K.A.1    Honig, B.2
  • 25
    • 0031578985 scopus 로고    scopus 로고
    • On the variational approach to the Poisson-Boltzmann free energies
    • Fogolari F, Briggs JM. On the variational approach to the Poisson-Boltzmann free energies. Chem Phys Lett 1997;281: 135-139.
    • (1997) Chem Phys Lett , vol.281 , pp. 135-139
    • Fogolari, F.1    Briggs, J.M.2
  • 26
    • 0029068766 scopus 로고
    • Polyelectrolyte electrostatics: Salt dependence, entropic and enthalpic contribution to free energy in the nonlinear Poisson-Boltzmann model
    • Sharp KA. Polyelectrolyte electrostatics: salt dependence, entropic and enthalpic contribution to free energy in the nonlinear Poisson-Boltzmann model. Biopolymers 1995;36:227-243.
    • (1995) Biopolymers , vol.36 , pp. 227-243
    • Sharp, K.A.1
  • 28
    • 0001585447 scopus 로고
    • Computation of electrostatic forces on solvated molecules using the Poisson-Boltzmann equation
    • Gilson MK, Davis ME, Luty BA, McCammon JA. Computation of electrostatic forces on solvated molecules using the Poisson-Boltzmann equation, J Phys Chem 1993;97:3591-3600.
    • (1993) J Phys Chem , vol.97 , pp. 3591-3600
    • Gilson, M.K.1    Davis, M.E.2    Luty, B.A.3    McCammon, J.A.4
  • 29
    • 0025197061 scopus 로고
    • a's of ionizable groups in proteins: Atomic detail from a continuum electrostatic model
    • a's of ionizable groups in proteins: atomic detail from a continuum electrostatic model. Biochemistry 1990;29:10219-10225.
    • (1990) Biochemistry , vol.29 , pp. 10219-10225
    • Bashford, D.1    Karplus, M.2
  • 30
    • 0028305457 scopus 로고
    • Prediction of pH-dependent properties of proteins
    • Antosiewicz J, McCammon JA, Gilson MK. Prediction of pH-dependent properties of proteins. J Mol Biol 1994;238:415-436.
    • (1994) J Mol Biol , vol.238 , pp. 415-436
    • Antosiewicz, J.1    McCammon, J.A.2    Gilson, M.K.3
  • 36
    • 0025398721 scopus 로고
    • WHATIF: A molecular modeling and drug design program
    • Vriend G. WHATIF: a molecular modeling and drug design program. J Mol Graphics 1990;8:52-56.
    • (1990) J Mol Graphics , vol.8 , pp. 52-56
    • Vriend, G.1
  • 37
    • 33748593093 scopus 로고    scopus 로고
    • Improving the continuum dielectric approach to calculating pKas of ionizable groups in proteins
    • Demchuck E, Wade R. Improving the continuum dielectric approach to calculating pKas of ionizable groups in proteins. J Phys Chem 1996;100:17373-17387.
    • (1996) J Phys Chem , vol.100 , pp. 17373-17387
    • Demchuck, E.1    Wade, R.2
  • 38
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectra analysis of biological macromolecules
    • Bartels C, Xia T, Billeter M, Güntert P, Wüthrich K. The program XEASY for computer-supported NMR spectra analysis of biological macromolecules. J Biomol NMR 1995;5:1-10.
    • (1995) J Biomol NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 39
    • 0031738305 scopus 로고    scopus 로고
    • 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin
    • Qin BY, Creamer LK, Baker EN, Jameson GB. 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Lett 1998;438:272-8.
    • (1998) FEBS Lett , vol.438 , pp. 272-278
    • Qin, B.Y.1    Creamer, L.K.2    Baker, E.N.3    Jameson, G.B.4
  • 40
    • 0032006812 scopus 로고    scopus 로고
    • Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR
    • Mesgarzadeh A, Pfeiffer S, Engelke J, Lassen D, Ruterjans H. Bound water in apo and holo bovine heart fatty-acid-binding protein determined by heteronuclear NMR. Eur J Biochem 1998; 251:781-786
    • (1998) Eur J Biochem , vol.251 , pp. 781-786
    • Mesgarzadeh, A.1    Pfeiffer, S.2    Engelke, J.3    Lassen, D.4    Ruterjans, H.5
  • 41
    • 0024815231 scopus 로고
    • Interaction of fatty acids with beta-lactoglobulin and albumin from ruminant milk
    • Perez MD, de Villegas D, Sanchez L, Aranda P, Ena JM, Calvo M. Interaction of fatty acids with beta-lactoglobulin and albumin from ruminant milk. J Biochem 1989;106:1094-1097.
    • (1989) J Biochem , vol.106 , pp. 1094-1097
    • Perez, M.D.1    De Villegas, D.2    Sanchez, L.3    Aranda, P.4    Ena, J.M.5    Calvo, M.6
  • 42
    • 0029851894 scopus 로고    scopus 로고
    • Monitoring complexation between some proteins and naphtalene dye by electrospray mass spectrometry
    • Hamdan M, Curcuruto O, Molinari H, Zetta L, Ragona L. Monitoring complexation between some proteins and naphtalene dye by electrospray mass spectrometry. J Mass Spect 1996;31:1261-1264.
    • (1996) J Mass Spect , vol.31 , pp. 1261-1264
    • Hamdan, M.1    Curcuruto, O.2    Molinari, H.3    Zetta, L.4    Ragona, L.5
  • 44
    • 0001497241 scopus 로고
    • The reversible transformation of β-lactoglobulin at pH 7.5
    • Tanford C, Bunville LG, Nozaki Y. The reversible transformation of β-lactoglobulin at pH 7.5. J Am Chem Soc 1959;81:4032-4036.
    • (1959) J Am Chem Soc , vol.81 , pp. 4032-4036
    • Tanford, C.1    Bunville, L.G.2    Nozaki, Y.3
  • 45
    • 0000714568 scopus 로고
    • Physico-chemical comparison of β-lactoglobulins A and B
    • Tanford C, Nozaki Y. Physico-chemical comparison of β-lactoglobulins A and B. J Biol Chem 1959;234:2874-2877.
    • (1959) J Biol Chem , vol.234 , pp. 2874-2877
    • Tanford, C.1    Nozaki, Y.2


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