메뉴 건너뛰기




Volumn 8, Issue 3, 1999, Pages 554-561

Energetics of solvent and ligand-induced conformational changes in α- lactalbumin

Author keywords

Ca2+ binding; Calorimetry; Denaturation; Residual structure; Thermodynamic parameters; lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; CALCIUM BINDING PROTEIN; SOLVENT;

EID: 0033053602     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.3.554     Document Type: Article
Times cited : (75)

References (38)
  • 3
    • 0021143705 scopus 로고
    • Metal ion binding to the N and A conformers of bovine alpha-lactalbumin
    • Bratcher SC, Kronman MJ. 1984. Metal ion binding to the N and A conformers of bovine alpha-lactalbumin. J Biol Chem 295:10875-10886.
    • (1984) J Biol Chem , vol.295 , pp. 10875-10886
    • Bratcher, S.C.1    Kronman, M.J.2
  • 4
    • 0001447396 scopus 로고
    • α-Lactalbumin
    • Fox P, ed. London, UK: Elsevier Press
    • Brew K, Grobler JA. 1992. α-Lactalbumin. In: Fox P, ed. Advanced dairy chemistry. London, UK: Elsevier Press, pp 191-229.
    • (1992) Advanced Dairy Chemistry , pp. 191-229
    • Brew, K.1    Grobler, J.A.2
  • 8
    • 0027269511 scopus 로고
    • Pathway of disulfide-coupled unfolding and refolding of bovine α-Lactalbumin
    • Ewbank JJ, Creighton TE. 1993. Pathway of disulfide-coupled unfolding and refolding of bovine α-lactalbumin. Biochemistry 32:3677-3693.
    • (1993) Biochemistry , vol.32 , pp. 3677-3693
    • Ewbank, J.J.1    Creighton, T.E.2
  • 9
    • 0028174361 scopus 로고
    • Energetics of α-lactalbumin states: A calorimetric and statistical thermodynamic study
    • Griko YV, Freire E, Privalov PP. 1994a. Energetics of α-lactalbumin states: A calorimetric and statistical thermodynamic study. Biochemistry 33:1889-1901.
    • (1994) Biochemistry , vol.33 , pp. 1889-1901
    • Griko, Y.V.1    Freire, E.2    Privalov, P.P.3
  • 10
    • 0029157132 scopus 로고
    • The unfolding thermodynamics of c-type lysozymes: A calorimetric study of the heat de-naturation of equine lysozyme
    • Griko YV, Freire E, Privalov G, Van Dael H, Privalov PL. 1995. The unfolding thermodynamics of c-type lysozymes: A calorimetric study of the heat de-naturation of equine lysozyme. J Mol Biol 252:447-459.
    • (1995) J Mol Biol , vol.252 , pp. 447-459
    • Griko, Y.V.1    Freire, E.2    Privalov, G.3    Van Dael, H.4    Privalov, P.L.5
  • 11
    • 0028143230 scopus 로고
    • Residual structure in a staphylococcal nuclease fragment. Is it a molten globule and is its unfolding a first-order phase transition?
    • Griko YV, Gittis A, Lattman EE, Privalov PL. 1994b. Residual structure in a staphylococcal nuclease fragment. Is it a molten globule and is its unfolding a first-order phase transition? J Mol Biol 243:93-99.
    • (1994) J Mol Biol , vol.243 , pp. 93-99
    • Griko, Y.V.1    Gittis, A.2    Lattman, E.E.3    Privalov, P.L.4
  • 12
    • 0028329347 scopus 로고
    • Thermodynamic puzzle of apomyoglobin unfolding
    • Griko YV, Privalov PL. 1994. Thermodynamic puzzle of apomyoglobin unfolding. J Mol Biol 235:1318-1325.
    • (1994) J Mol Biol , vol.235 , pp. 1318-1325
    • Griko, Y.V.1    Privalov, P.L.2
  • 13
    • 0030036162 scopus 로고    scopus 로고
    • Large heat capacity change in a protein-monovalent cation interaction
    • Guinto ER, Di Cera E. 1996. Large heat capacity change in a protein-monovalent cation interaction. Biochemistry 35:8800-8804.
    • (1996) Biochemistry , vol.35 , pp. 8800-8804
    • Guinto, E.R.1    Di Cera, E.2
  • 15
    • 0029877043 scopus 로고    scopus 로고
    • Energetics of structural domains in α-lactalbumin
    • Hendrix TM, Griko YV, Privalov PL. 1996. Energetics of structural domains in α-lactalbumin. Protein Sci 5:923-931.
    • (1996) Protein Sci , vol.5 , pp. 923-931
    • Hendrix, T.M.1    Griko, Y.V.2    Privalov, P.L.3
  • 16
    • 0021430496 scopus 로고
    • Thermodynamics of thermal unfolding of bovine apo-α-lactalhumin
    • Hiraoka Y, Sugai S. 1984. Thermodynamics of thermal unfolding of bovine apo-α-lactalhumin. Int J Pept Protein Res 23:535-542.
    • (1984) Int J Pept Protein Res , vol.23 , pp. 535-542
    • Hiraoka, Y.1    Sugai, S.2
  • 17
    • 0022122037 scopus 로고
    • Equilibrium and kinetic study of sodium and potassium-induced conformational changes of apo-α-lactalbumin
    • Hiraoka Y, Sugai S. 1985. Equilibrium and kinetic study of sodium and potassium-induced conformational changes of apo-α-lactalbumin. Int J Pept Protein Res 26:252-261.
    • (1985) Int J Pept Protein Res , vol.26 , pp. 252-261
    • Hiraoka, Y.1    Sugai, S.2
  • 18
    • 0023041667 scopus 로고
    • Evidence for identity between the equilibrium intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme
    • Ikeguchi M, Kuwajima K, Mitani M, Sugai S. 1986. Evidence for identity between the equilibrium intermediate and a transient folding intermediate: A comparative study of the folding reactions of α-lactalbumin and lysozyme. Biochemistry 25:6965-6972.
    • (1986) Biochemistry , vol.25 , pp. 6965-6972
    • Ikeguchi, M.1    Kuwajima, K.2    Mitani, M.3    Sugai, S.4
  • 19
    • 0024796120 scopus 로고
    • Metal-ion binding and the molecular conformational properties of α-lactalbumin
    • Kronman MJ. 1989. Metal-ion binding and the molecular conformational properties of α-lactalbumin. Crit Rev Biochem Mol Biol 24:565-667.
    • (1989) Crit Rev Biochem Mol Biol , vol.24 , pp. 565-667
    • Kronman, M.J.1
  • 21
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure
    • Kuwajima K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure. Proteins 6:87-103.
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 22
    • 0022559769 scopus 로고
    • 2- binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra
    • 2- binding on the structure and stability of bovine α-lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra. Int J Pept Protein Res 27:18-27.
    • (1986) Int J Pept Protein Res , vol.27 , pp. 18-27
    • Kuwajima, K.1    Harushima, Y.2    Sugai, S.3
  • 23
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
    • Kuwajima K, Hiraoka Y, Ikeguchi M, Sugai S. 1985. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry 24:874-881.
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0025811817 scopus 로고
    • Lysozyme and α-lactalbumin: Structure, function and interrelationships
    • Mckenzie HA, White FH Jr. 1991. Lysozyme and α-lactalbumin: Structure, function and interrelationships. Adv Protein Chem 41:173-315.
    • (1991) Adv Protein Chem , vol.41 , pp. 173-315
    • McKenzie, H.A.1    White F.H., Jr.2
  • 26
    • 78651163419 scopus 로고
    • Disc-electrophoresis - I. Background and theory
    • Ornstein L. 1964. Disc-electrophoresis - I. Background and theory. Ann NY Acad Sci 121:321-349.
    • (1964) Ann NY Acad Sci , vol.121 , pp. 321-349
    • Ornstein, L.1
  • 27
    • 0021979565 scopus 로고
    • Cation binding effect on the pH, thermal and urea denaturation transitions in α-lactalbumin
    • Permyakov EA, Morozova LA, Burstein EA. 1985. Cation binding effect on the pH, thermal and urea denaturation transitions in α-lactalbumin. Biophys Chem 21:21-31.
    • (1985) Biophys Chem , vol.21 , pp. 21-31
    • Permyakov, E.A.1    Morozova, L.A.2    Burstein, E.A.3
  • 28
    • 0008750928 scopus 로고
    • A scanning calorimetric study of bovine and human apo-α-lactalbumin
    • Pfeil W, Sadowski ML. 1985. A scanning calorimetric study of bovine and human apo-α-lactalbumin. Stadia Biophysica 109:163-170.
    • (1985) Stadia Biophysica , vol.109 , pp. 163-170
    • Pfeil, W.1    Sadowski, M.L.2
  • 29
    • 0025287103 scopus 로고
    • Heat capacity of proteins. II partial molar heat capacity of the unfolded polypeptide chains of proteins: Protein unfolding effects
    • Privalov PL, Makhatadze GI. 1990. Heat capacity of proteins. II Partial molar heat capacity of the unfolded polypeptide chains of proteins: Protein unfolding effects. J Mol Biol 213:385-391.
    • (1990) J Mol Biol , vol.213 , pp. 385-391
    • Privalov, P.L.1    Makhatadze, G.I.2
  • 30
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature induced changes in proteins
    • Privalov PL, Potekhin SA. 1986. Scanning microcalorimetry in studying temperature induced changes in proteins. Methods Enzymol 131:4-51.
    • (1986) Methods Enzymol , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 31
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton TE, ed. New York: WH Freeman
    • Ptitsyn OB. 1992. The molten globule state. In: Creighton TE, ed. Protein folding. New York: WH Freeman. pp 243-300.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 32
    • 24444434350 scopus 로고
    • Thermodynamic parameters of jβ-lactoglobulin and α-lactalbumin. A DSC study of denaturation by heating
    • Relkin P, Eynard L, Launay B. 1992. Thermodynamic parameters of jβ-lactoglobulin and α-lactalbumin. A DSC study of denaturation by heating. Thermochim Acta 204:111-121.
    • (1992) Thermochim Acta , vol.204 , pp. 111-121
    • Relkin, P.1    Eynard, L.2    Launay, B.3
  • 33
    • 0021696161 scopus 로고
    • Interaction of galoctosyltransferase with α-lactalbumin and substrates
    • Takase K, Ebner KE. 1984. Interaction of galoctosyltransferase with α-lactalbumin and substrates. Curr Top Cell Rec 24:51-62.
    • (1984) Curr Top Cell Rec , vol.24 , pp. 51-62
    • Takase, K.1    Ebner, K.E.2
  • 35
    • 0012015424 scopus 로고
    • Osmometry and general characterization of α-lactalbumin
    • Wetlaufer DB. 1961. Osmometry and general characterization of α-lactalbumin. C R Trav Lab Carlsberg 32:125-138.
    • (1961) C R Trav Lab Carlsberg , vol.32 , pp. 125-138
    • Wetlaufer, D.B.1
  • 36
    • 0024356301 scopus 로고
    • Rapid measurements of binding constants and heals of binding using a new titration calorimeter
    • Wiseman T, Williston S, Brants JF, Lin LN. 1989. Rapid measurements of binding constants and heals of binding using a new titration calorimeter. Anal Biochem 179:131-137.
    • (1989) Anal Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brants, J.F.3    Lin, L.N.4
  • 37
    • 0030025082 scopus 로고    scopus 로고
    • Disulfide determinants of calcium-induced packing in α-lactalbumin
    • Wu LC, Schulman BA, Peng Z-Y, Kim PS. 1996. Disulfide determinants of calcium-induced packing in α-lactalbumin. Biochemistry 35:859-863.
    • (1996) Biochemistry , vol.35 , pp. 859-863
    • Wu, L.C.1    Schulman, B.A.2    Peng, Z.-Y.3    Kim, P.S.4
  • 38
    • 0026330844 scopus 로고
    • Calorimetric determination of the energetics of the molten globule intermediate in protein folding: Apo-α-lactalbumin
    • Xie D, Buakuni V, Freire E. 1991. Calorimetric determination of the energetics of the molten globule intermediate in protein folding: Apo-α-lactalbumin. Biochemistry 30:10673-10672.
    • (1991) Biochemistry , vol.30 , pp. 10673-110672
    • Xie, D.1    Buakuni, V.2    Freire, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.