메뉴 건너뛰기




Volumn 264, Issue 4, 1996, Pages 806-822

The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy

Author keywords

Circular dichroism; Folding intermediate; Protein folding; Stopped flow; lactoglobulin

Indexed keywords

BETA LACTOGLOBULIN; GLOBULAR PROTEIN; GUANIDINE;

EID: 0030582679     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0678     Document Type: Article
Times cited : (122)

References (95)
  • 1
    • 0015212906 scopus 로고
    • A comparison of the denaturation of bovine β-lactoglobulin A and B and goat β-lactoglobulin
    • Alexander, S. S. & Pace, C. N. (1971). A comparison of the denaturation of bovine β-lactoglobulin A and B and goat β-lactoglobulin. Biochemistry, 10, 2738-2743.
    • (1971) Biochemistry , vol.10 , pp. 2738-2743
    • Alexander, S.S.1    Pace, C.N.2
  • 2
    • 0030348041 scopus 로고    scopus 로고
    • Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
    • Arai, M. & Kuwajima, K. (1996). Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Fold. De. 1, 275-287.
    • (1996) Fold. De. , vol.1 , pp. 275-287
    • Arai, M.1    Kuwajima, K.2
  • 4
    • 0027394285 scopus 로고
    • Pulsed H/D-exchange studies of folding intermediates
    • Baldwin, R. L. (1993). Pulsed H/D-exchange studies of folding intermediates. Curr. Opin. Struct. Biol. 3, 84-91.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 84-91
    • Baldwin, R.L.1
  • 5
    • 0028387381 scopus 로고
    • Finding intermediates in protein folding
    • Baldwin, R. L. (1994). Finding intermediates in protein folding. BioEssays, 16, 207-210.
    • (1994) BioEssays , vol.16 , pp. 207-210
    • Baldwin, R.L.1
  • 6
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin, R. L. (1995). The nature of protein folding pathways: the classical versus the new view. J. Biomol. NMR, 5, 103-109.
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 7
    • 0027254057 scopus 로고
    • The molten globule intermediate of apomyoglobin and the process of protein folding
    • Barrick, D. & Baldwin, R. L. (1993). The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci. 2, 869-876.
    • (1993) Protein Sci. , vol.2 , pp. 869-876
    • Barrick, D.1    Baldwin, R.L.2
  • 11
    • 0030342681 scopus 로고    scopus 로고
    • Conformational switching in designed peptides: The helix/sheet transition
    • Cerpa, R., Cohen, F. E. & Kuntz, I. D. (1996). Conformational switching in designed peptides: the helix/sheet transition. Fold. Des. 1, 91-101.
    • (1996) Fold. Des. , vol.1 , pp. 91-101
    • Cerpa, R.1    Cohen, F.E.2    Kuntz, I.D.3
  • 13
    • 0026793589 scopus 로고
    • Kinetic resolution of peptide bond and side-chain far-UV circular dichroism during the folding of hen egg white lysozyme
    • Chaffotte, A. F., Guillou, Y. & Goldberg, M. E. (1992). Kinetic resolution of peptide bond and side-chain far-UV circular dichroism during the folding of hen egg white lysozyme. Biochemistry, 31, 9694-9702.
    • (1992) Biochemistry , vol.31 , pp. 9694-9702
    • Chaffotte, A.F.1    Guillou, Y.2    Goldberg, M.E.3
  • 14
    • 0003103643 scopus 로고
    • Determination of the helix and β form of proteins in aqueous solution by circular dichroism
    • Chen, Y. H., Yang, J. T. & Chau, K. H. (1974). Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry, 20, 33-37.
    • (1974) Biochemistry , vol.20 , pp. 33-37
    • Chen, Y.H.1    Yang, J.T.2    Chau, K.H.3
  • 15
    • 0028965716 scopus 로고
    • Impact of esterification on the folding and the susceptibility to peptic proteolysis of β-lactoglobulin
    • Chobert, J.-M., Briand, L., Grinberg, V. & Haertlè, T. (1995). Impact of esterification on the folding and the susceptibility to peptic proteolysis of β-lactoglobulin. Biochim. Biophys. Acta, 1248, 170-176.
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 170-176
    • Chobert, J.-M.1    Briand, L.2    Grinberg, V.3    Haertlè, T.4
  • 16
    • 0014428424 scopus 로고
    • The optical activity of the disulfide bond in L-cystine and some derivatives of L-cystine
    • Coleman, D. L. & Blout, E. R. (1968). The optical activity of the disulfide bond in L-cystine and some derivatives of L-cystine. J. Am. Chem. Soc. 90, 2405-2416.
    • (1968) J. Am. Chem. Soc. , vol.90 , pp. 2405-2416
    • Coleman, D.L.1    Blout, E.R.2
  • 17
    • 0028989022 scopus 로고
    • Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin
    • Creamer, L. K. (1995). Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin. Biochemistry, 34, 7170-7176.
    • (1995) Biochemistry , vol.34 , pp. 7170-7176
    • Creamer, L.K.1
  • 20
    • 0001877468 scopus 로고
    • Characterization of protein folding intermediates
    • Dobson, C. M. (1991). Characterization of protein folding intermediates. Curr. Opin. Struct. Biol. 1, 22-27.
    • (1991) Curr. Opin. Struct. Biol. , vol.1 , pp. 22-27
    • Dobson, C.M.1
  • 21
    • 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. (1996). Infrared and circular dichroism spectroscopic characterization of structural differences between β-lactoglobulin A and B. Biochemistry, 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
  • 22
    • 0025603181 scopus 로고
    • Alcohol-induced changes of β-lactoglobulin-retinol-binding stoichiometry
    • Dufour, E. & Haertlè, T. (1990). Alcohol-induced changes of β-lactoglobulin-retinol-binding stoichiometry. Protein Eng. 4, 185-190.
    • (1990) Protein Eng. , vol.4 , pp. 185-190
    • Dufour, E.1    Haertlè, T.2
  • 23
    • 0027376117 scopus 로고
    • Temperature-induced folding changes of β-lactoglobulin in hydromethanolic solutions
    • Dufour, E. & Haertlè, T. (1993). Temperature-induced folding changes of β-lactoglobulin in hydromethanolic solutions. Int. J. Biol. Macromol. 15, 293-297.
    • (1993) Int. J. Biol. Macromol. , vol.15 , pp. 293-297
    • Dufour, E.1    Haertlè, T.2
  • 24
    • 0027578704 scopus 로고
    • Reversible effects of medium dielectric constant on structural transformation of β-lactoglobulin and its retinol binding
    • Dufour, E., Bertrand-Harb, C. & Haertlè, T. (1993). Reversible effects of medium dielectric constant on structural transformation of β-lactoglobulin and its retinol binding. Biopolymers, 33, 589-598.
    • (1993) Biopolymers , vol.33 , pp. 589-598
    • Dufour, E.1    Bertrand-Harb, C.2    Haertlè, T.3
  • 25
    • 0028179225 scopus 로고
    • Conformation changes of β-lactoglobulin: An ATR infrared spectroscopic study of the effect of pH and ethanol
    • Dufour, E., Robert, P., Bertrand, D. & Haertlè, T. (1994). Conformation changes of β-lactoglobulin: an ATR infrared spectroscopic study of the effect of pH and ethanol. J. Protein Chem. 13, 143-150.
    • (1994) J. Protein Chem. , vol.13 , pp. 143-150
    • Dufour, E.1    Robert, P.2    Bertrand, D.3    Haertlè, T.4
  • 26
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander, S. W. & Mayne, L. (1992). Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu. Rev. Biophys. Biomol. Struct. 21, 243-265.
    • (1992) Annu. Rev. Biophys. Biomol. Struct. , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 27
    • 0028856785 scopus 로고
    • Optimization of rates of protein folding: The nucleation-condensation mechanism and its implications
    • Fersht, A. R. (1995). Optimization of rates of protein folding: the nucleation-condensation mechanism and its implications. Proc. Natl Acad. Sci. USA, 92, 10869-10873.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10869-10873
    • Fersht, A.R.1
  • 28
    • 0029157429 scopus 로고
    • Compact intermediate states in protein folding
    • Fink, A. L. (1995). Compact intermediate states in protein folding. Annu. Rev. Biophys. Biomol. Struct. 24, 495-522.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 495-522
    • Fink, A.L.1
  • 29
    • 0026019655 scopus 로고
    • Rate of β-structure formation in polypeptides
    • Finkelstein, A. V. (1991). Rate of β-structure formation in polypeptides. Proteins: Struct. Funct. Genet. 9, 23-27.
    • (1991) Proteins: Struct. Funct. Genet. , vol.9 , pp. 23-27
    • Finkelstein, A.V.1
  • 30
    • 0023960321 scopus 로고
    • The structural motif of β-lactoglobulin and retinol-binding protein: A basic framework for binding and transport of small hydrophobic molecules?
    • Godovac-Zimmermann, J. (1988). The structural motif of β-lactoglobulin and retinol-binding protein: a basic framework for binding and transport of small hydrophobic molecules? Trends Biochem. Sci. 13, 64-66.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 64-66
    • Godovac-Zimmermann, J.1
  • 31
    • 0021874876 scopus 로고
    • Homology between the primary structures of β-lactoglobulins and human retinol-binding protein: Evidence for a similar biological function?
    • Godovac-Zimmermann, J., Conti, A., Liberatori, J. & Braunitzer, G. (1985). Homology between the primary structures of β-lactoglobulins and human retinol-binding protein: Evidence for a similar biological function? Biol. Chem. Hoppe Seyler, 366, 431-434.
    • (1985) Biol. Chem. Hoppe Seyler , vol.366 , pp. 431-434
    • Godovac-Zimmermann, J.1    Conti, A.2    Liberatori, J.3    Braunitzer, G.4
  • 32
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. J. & Fasman, G. D. (1969). Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry, 8, 4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.J.1    Fasman, G.D.2
  • 33
    • 0026774488 scopus 로고
    • Calorimetric study of the heat and cold denaturation of β-lactoglobulin
    • Griko, Y. V. & Privalov, P. L. (1992). Calorimetric study of the heat and cold denaturation of β-lactoglobulin. Biochemistry, 31, 8810-8815.
    • (1992) Biochemistry , vol.31 , pp. 8810-8815
    • Griko, Y.V.1    Privalov, P.L.2
  • 34
    • 0028944346 scopus 로고
    • Is burst hydrophobic collapse necessary for protein folding?
    • Gutin, A. M., Abkevich, V. I. & Shakhnovich, E. I. (1995). Is burst hydrophobic collapse necessary for protein folding? Biochemistry, 34, 3066-3076.
    • (1995) Biochemistry , vol.34 , pp. 3066-3076
    • Gutin, A.M.1    Abkevich, V.I.2    Shakhnovich, E.I.3
  • 35
    • 0029588554 scopus 로고
    • High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein
    • Hamada, D., Kuroda, Y., Tanaka, T. & Goto, Y. (1995). High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein. J. Mol. Biol. 254, 737-746.
    • (1995) J. Mol. Biol. , vol.254 , pp. 737-746
    • Hamada, D.1    Kuroda, Y.2    Tanaka, T.3    Goto, Y.4
  • 37
    • 0023855264 scopus 로고
    • An analysis of the 225-230-nm CD band of elapid toxins
    • Hider, R. C., Drake, A. F. & Tamiya, N. (1988a). An analysis of the 225-230-nm CD band of elapid toxins. Biopolymers, 27, 113-122.
    • (1988) Biopolymers , vol.27 , pp. 113-122
    • Hider, R.C.1    Drake, A.F.2    Tamiya, N.3
  • 38
    • 0023770156 scopus 로고
    • Origin of the positive 225-230 nm circular dichroism band in proteins. Its application to conformational analysis
    • Hider, R. C., Kupryszewski, G., Rekowski, P. & Lammek, B. (1988b). Origin of the positive 225-230 nm circular dichroism band in proteins. Its application to conformational analysis. Biophys. Chem. 31, 45-51.
    • (1988) Biophys. Chem. , vol.31 , pp. 45-51
    • Hider, R.C.1    Kupryszewski, G.2    Rekowski, P.3    Lammek, B.4
  • 39
    • 0028232822 scopus 로고
    • The refolding of human lysozyme: A comparison with the structurally homologous hen lysozyme
    • Hooke, S. D., Radford, S. E. & Dobson, C. M. (1994). The refolding of human lysozyme: a comparison with the structurally homologous hen lysozyme. Biochemistry, 33, 5867-5876.
    • (1994) Biochemistry , vol.33 , pp. 5867-5876
    • Hooke, S.D.1    Radford, S.E.2    Dobson, C.M.3
  • 40
    • 0028008617 scopus 로고
    • Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy
    • Jacobs, M. D. & Fox, R. O. (1994). Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy. Proc. Natl Acad. Sci. USA, 91, 449-453.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 449-453
    • Jacobs, M.D.1    Fox, R.O.2
  • 41
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P. A. & Wright, P. E. (1993). Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science, 262, 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 42
    • 0028947956 scopus 로고
    • Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR
    • Jones, B. E. & Matthews, C. R. (1995). Early intermediates in the folding of dihydrofolate reductase from Escherichia coli detected by hydrogen exchange and NMR. Protein Sci. 4, 167-177.
    • (1995) Protein Sci. , vol.4 , pp. 167-177
    • Jones, B.E.1    Matthews, C.R.2
  • 43
    • 0028168283 scopus 로고
    • Tryptophan-19 of β-lactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure
    • Katakura, Y., Totsuka, M., Ametani, A. & Kaminogawa, S. (1994). Tryptophan-19 of β-lactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure. Biochim. Biophys. Acta, 1207, 58-67.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 58-67
    • Katakura, Y.1    Totsuka, M.2    Ametani, A.3    Kaminogawa, S.4
  • 44
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • Kiefhaber, T. (1995). Kinetic traps in lysozyme folding. Proc. Natl Acad. Sci. USA, 92, 9029-9033.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 45
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P. S. & Baldwin, R. L. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 46
    • 0027370063 scopus 로고
    • Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization
    • Koide, S., Dyson, H. J. & Wright, P. E. (1993). Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization. Biochemistry, 32, 12299-12310.
    • (1993) Biochemistry , vol.32 , pp. 12299-12310
    • Koide, S.1    Dyson, H.J.2    Wright, P.E.3
  • 47
    • 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: Struct. Funct. Genet. 6, 87-103.
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 48
    • 0029174217 scopus 로고
    • Circular dichroism
    • (Shirley, B. A., ed.), Humana Press Inc. Totowa, NJ
    • Kuwajima, K. (1995). Circular dichroism. In Protein Stability and Folding. Methods in Molecular Biology (Shirley, B. A., ed.), vol. 40, pp. 115-135, Humana Press Inc. Totowa, NJ.
    • (1995) Protein Stability and Folding. Methods in Molecular Biology , vol.40 , pp. 115-135
    • Kuwajima, K.1
  • 49
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of α-lactalbumin
    • Kuwajima, K. (1996a). The molten globule state of α-lactalbumin. FASEB J. 10, 102-109.
    • (1996) FASEB J. , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 51
    • 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
  • 52
    • 0023669402 scopus 로고
    • Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism
    • Kuwajima, K., Yamaya, H., Miwa, S., Sugai, S. & Nagamura, T. (1987). Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism. FEBS Letters, 221, 115-118.
    • (1987) FEBS Letters , vol.221 , pp. 115-118
    • Kuwajima, K.1    Yamaya, H.2    Miwa, S.3    Sugai, S.4    Nagamura, T.5
  • 53
    • 0023772234 scopus 로고
    • Folding of carp parvalbumin studied by equilibrium and kinetic circular dichroism spectra
    • Kuwajima, K., Sakuraoka, A., Fueki, S., Yoneyama, M. & Sugai, S. (1988). Folding of carp parvalbumin studied by equilibrium and kinetic circular dichroism spectra. Biochemistry, 27, 7419-7428.
    • (1988) Biochemistry , vol.27 , pp. 7419-7428
    • Kuwajima, K.1    Sakuraoka, A.2    Fueki, S.3    Yoneyama, M.4    Sugai, S.5
  • 54
    • 0027432676 scopus 로고
    • Secondary structure of globular proteins at the early and the final stages in protein folding
    • Kuwajima, K., Semisotnov, G. V., Finkelstein, A. V., Sugai, S. & Ptitsyn, O. B. (1993). Secondary structure of globular proteins at the early and the final stages in protein folding. FEBS Letters, 334, 265-268.
    • (1993) FEBS Letters , vol.334 , pp. 265-268
    • Kuwajima, K.1    Semisotnov, G.V.2    Finkelstein, A.V.3    Sugai, S.4    Ptitsyn, O.B.5
  • 55
    • 0017822195 scopus 로고
    • Polypeptide chain folding through a highly helical intermediate as a general principle of globular protein structure formation
    • Lim, V. I. (1978). Polypeptide chain folding through a highly helical intermediate as a general principle of globular protein structure formation. FEBS Letters, 89, 10-14.
    • (1978) FEBS Letters , vol.89 , pp. 10-14
    • Lim, V.I.1
  • 56
    • 0028040301 scopus 로고
    • Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly β-sheet protein
    • Liu, Z. P., Rizo, J. & Gierasch, L. M. (1994). Equilibrium folding studies of cellular retinoic acid binding protein, a predominantly β-sheet protein. Biochemistry, 33, 134-142.
    • (1994) Biochemistry , vol.33 , pp. 134-142
    • Liu, Z.P.1    Rizo, J.2    Gierasch, L.M.3
  • 57
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh, S. N., Kay, M. S. & Baldwin, R. L. (1995). Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl Acad. Sci. USA, 92, 5446-5450.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 58
    • 0027389744 scopus 로고
    • Characterization of folding intermediates of human carbonic anhydrase II: Probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis
    • Mårtensson, L. G., Jonsson, B. H., Freskgård, P. O., Kihlgren, A., Svensson, M. & Carlsson, U. (1993). Characterization of folding intermediates of human carbonic anhydrase II: probing substructure by chemical labeling of SH groups introduced by site-directed mutagenesis. Biochemistry, 32, 224-231.
    • (1993) Biochemistry , vol.32 , pp. 224-231
    • Mårtensson, L.G.1    Jonsson, B.H.2    Freskgård, P.O.3    Kihlgren, A.4    Svensson, M.5    Carlsson, U.6
  • 59
    • 0027313673 scopus 로고
    • Pathways of protein folding
    • Matthews, C. R. (1993). Pathways of protein folding. Annu. Rev. Biochem. 62, 653-683.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 653-683
    • Matthews, C.R.1
  • 60
    • 0015922140 scopus 로고
    • Bovine β-lactglobulins in urea solution. Denaturation at pH 5.2 and 3.5
    • McKenzie, H. A. & Ralston, G. B. (1973). Bovine β-lactglobulins in urea solution. Denaturation at pH 5.2 and 3.5. Biochemistry, 12, 1025-1034.
    • (1973) Biochemistry , vol.12 , pp. 1025-1034
    • McKenzie, H.A.1    Ralston, G.B.2
  • 61
    • 0029865623 scopus 로고    scopus 로고
    • Context-dependent secondary structure formation of a designed protein sequence
    • Minor, D. L., Jr & Kim, P. S. (1996). Context-dependent secondary structure formation of a designed protein sequence. Nature, 380, 730-734.
    • (1996) Nature , vol.380 , pp. 730-734
    • Minor D.L., Jr.1    Kim, P.S.2
  • 62
    • 0027770910 scopus 로고
    • Detection of transient protein folding populations by mass spectrometry
    • Miranker, A., Robinson, C. V., Radford, S. E., Aplin, R. T. & Dobson, C. M. (1993). Detection of transient protein folding populations by mass spectrometry. Science, 262, 896-900.
    • (1993) Science , vol.262 , pp. 896-900
    • Miranker, A.1    Robinson, C.V.2    Radford, S.E.3    Aplin, R.T.4    Dobson, C.M.5
  • 64
    • 0026848943 scopus 로고
    • Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity
    • Monaco, H. L. & Zanotti, G. (1992). Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity. Biopolymers, 32, 457-465.
    • (1992) Biopolymers , vol.32 , pp. 457-465
    • Monaco, H.L.1    Zanotti, G.2
  • 65
    • 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. & Eliopoulos, E. E. (1987). Crystal structure of the trigonal form of bovine β-lactoglobulin and its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 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    Eliopoulos, E.E.6
  • 66
    • 0026643282 scopus 로고
    • Analysis of the two-state behavior of the thermal unfolding of serum retinol binding protein containing a single retinol ligand
    • Muccio, D. D., Waterhous, D. V., Fish, F. & Brouillette, C. G. (1992). Analysis of the two-state behavior of the thermal unfolding of serum retinol binding protein containing a single retinol ligand. Biochemistry, 31, 5560-5567.
    • (1992) Biochemistry , vol.31 , pp. 5560-5567
    • Muccio, D.D.1    Waterhous, D.V.2    Fish, F.3    Brouillette, C.G.4
  • 67
    • 0026326273 scopus 로고
    • Predicting protein secondary structure based on amino acid sequence
    • Nishikawa, K. & Noguchi, T. (1991). Predicting protein secondary structure based on amino acid sequence. Methods Enzymol. 202, 31-44.
    • (1991) Methods Enzymol. , vol.202 , pp. 31-44
    • Nishikawa, K.1    Noguchi, T.2
  • 68
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. (1986). Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131, 266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 69
    • 0014226043 scopus 로고
    • Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 55°
    • Pace, C. N. & Tanford, C. (1968). Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 55°. Biochemistry, 7, 198-208.
    • (1968) Biochemistry , vol.7 , pp. 198-208
    • Pace, C.N.1    Tanford, C.2
  • 70
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G. & Gray, T. (1995). How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 72
    • 0029302371 scopus 로고
    • Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: A review
    • Ferez, M. D. & Calvo, M. (1994). Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: A review. J. Dairy Sci. 78, 978-988.
    • (1994) J. Dairy Sci. , vol.78 , pp. 978-988
    • Ferez, M.D.1    Calvo, M.2
  • 73
    • 0021876620 scopus 로고
    • Homology of β-lactoglobulin, serum retinol-binding protein, and protein HC
    • Pervaiz, S. & Brew, K. (1985). Homology of β-lactoglobulin, serum retinol-binding protein, and protein HC. Science, 228, 335-337.
    • (1985) Science , vol.228 , pp. 335-337
    • Pervaiz, S.1    Brew, K.2
  • 74
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn, O. B. (1995). Molten globule and protein folding. Advan. Protein Chem. 47, 83-229.
    • (1995) Advan. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 75
    • 0027406036 scopus 로고
    • Mechanism of pH-induced release of retinol from retinol-binding protein
    • Ptitsyn, O. B., Zanotti, G., Denesyuk, A. L. & Bychkova, V. E. (1993). Mechanism of pH-induced release of retinol from retinol-binding protein. FEBS Letters, 317, 181-184.
    • (1993) FEBS Letters , vol.317 , pp. 181-184
    • Ptitsyn, O.B.1    Zanotti, G.2    Denesyuk, A.L.3    Bychkova, V.E.4
  • 76
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S. E., Dobson, C. M. & Evans, P. A. (1992). The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature, 358, 302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 77
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
    • Roder, H., Elöve, G. A. & Englander, S. W. (1988). Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature, 335, 700-704.
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 78
    • 0024446515 scopus 로고
    • Unusual far-ultraviolet circular dichroism of wheat germ agglutinin and hevein originated from cystine residues
    • Rodríguez-Romero, A., Arreguín, B. & Hernández-Arana, A. (1989). Unusual far-ultraviolet circular dichroism of wheat germ agglutinin and hevein originated from cystine residues. Biochim. Biophys. Acta, 998, 21-24.
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 21-24
    • Rodríguez-Romero, A.1    Arreguín, B.2    Hernández-Arana, A.3
  • 80
    • 0027684807 scopus 로고
    • The secondary structure of milk proteins and their biological function
    • Sawyer, L. & Holt, C. (1993). The secondary structure of milk proteins and their biological function. J. Dairy Sci. 76, 3062-3078.
    • (1993) J. Dairy Sci. , vol.76 , pp. 3062-3078
    • Sawyer, L.1    Holt, C.2
  • 81
    • 0015057050 scopus 로고
    • A new basis for interpreting the circular dichroic spectra of proteins
    • Saxena, V. P. & Wetlaufer, D. B. (1971). A new basis for interpreting the circular dichroic spectra of proteins. Proc. Natl Acad. Sci. USA, 68, 969-972.
    • (1971) Proc. Natl Acad. Sci. USA , vol.68 , pp. 969-972
    • Saxena, V.P.1    Wetlaufer, D.B.2
  • 83
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of the α -helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
    • Shiraki, K., Nishikawa, K. & Goto, Y. (1995). Trifluoroethanol-induced stabilization of the α -helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245, 180-194.
    • (1995) J. Mol. Biol. , vol.245 , pp. 180-194
    • Shiraki, K.1    Nishikawa, K.2    Goto, Y.3
  • 85
    • 0029940033 scopus 로고    scopus 로고
    • Molecular collapse: The rate-limiting step in two-state cytochrome c folding
    • Sosnick, T. R., Mayne, L. & Englander, S. W. (1996). Molecular collapse: The rate-limiting step in two-state cytochrome c folding. Proteins: Struct. Fund. Genet. 24, 413-426.
    • (1996) Proteins: Struct. Fund. Genet. , vol.24 , pp. 413-426
    • Sosnick, T.R.1    Mayne, L.2    Englander, S.W.3
  • 86
    • 0029058420 scopus 로고
    • Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues
    • Svensson, M., Jonasson, P., Freskgård, P. O., Jonsson, B. H., Lindgren, M., Mårtensson, L. G., Gentile, M., Borèn, K. & Carlsson, U. (1995). Mapping the folding intermediate of human carbonic anhydrase II. Probing substructure by chemical reactivity and spin and fluorescence labeling of engineered cysteine residues. Biochemistry, 34, 8606-8620.
    • (1995) Biochemistry , vol.34 , pp. 8606-8620
    • Svensson, M.1    Jonasson, P.2    Freskgård, P.O.3    Jonsson, B.H.4    Lindgren, M.5    Mårtensson, L.G.6    Gentile, M.7    Borèn, K.8    Carlsson, U.9
  • 87
    • 0025695803 scopus 로고
    • Circular dichroism studies on helical structure preferences of amino acid residues of proteins caused by sodium dodecyl sulfate
    • Takeda, K. & Moriyama, Y. (1990). Circular dichroism studies on helical structure preferences of amino acid residues of proteins caused by sodium dodecyl sulfate. J. Protein Chem. 9, 573-582.
    • (1990) J. Protein Chem. , vol.9 , pp. 573-582
    • Takeda, K.1    Moriyama, Y.2
  • 88
    • 0001415860 scopus 로고
    • The role of the α-helix in the structure of proteins. Optical rotatory dispersion of β-lactoglobulin
    • Tanford, C., De, P. K. & Taggart, V. G. (1960). The role of the α-helix in the structure of proteins. Optical rotatory dispersion of β-lactoglobulin. J. Am. Chem. Soc. 82, 6028-6034.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 6028-6034
    • Tanford, C.1    De, P.K.2    Taggart, V.G.3
  • 89
    • 0014027395 scopus 로고
    • The optical rotatory dispersion of the β-lactoglobulins
    • Timasheff, S. N., Townend, R. & Mescanti, L. (1966). The optical rotatory dispersion of the β-lactoglobulins. J. Biol. Chem. 241, 1863-1870.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1863-1870
    • Timasheff, S.N.1    Townend, R.2    Mescanti, L.3
  • 90
    • 0000819131 scopus 로고
    • Molecular interactions in β-lactoglobulin. II. Ultracentrifugation and electrophoretic studies of the association of β-lactoglobulin below its isoelectric point
    • Townend, R., Winterbottom, R. J. & Timasheff, S. N. (1960). Molecular interactions in β-lactoglobulin. II. Ultracentrifugation and electrophoretic studies of the association of β-lactoglobulin below its isoelectric point. J. Am. Chem. Soc. 82, 3161-3168.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 3161-3168
    • Townend, R.1    Winterbottom, R.J.2    Timasheff, S.N.3
  • 92
    • 0028279006 scopus 로고
    • Importance of environment in determining secondary structure in proteins
    • Waterhous, D. V. & Johnson, W. C., Jr (1994). Importance of environment in determining secondary structure in proteins. Biochemistry, 33, 2121-2128.
    • (1994) Biochemistry , vol.33 , pp. 2121-2128
    • Waterhous, D.V.1    Johnson W.C., Jr.2
  • 93
    • 0002439879 scopus 로고
    • Circular dichroism of peptides
    • (Udenfried, S., Meienhofer, J. & Hruby, V. J., eds), Academic Press, San Diego
    • Woody, R. W. (1985). Circular dichroism of peptides. In The Peptides (Udenfried, S., Meienhofer, J. & Hruby, V. J., eds), vol. 7, pp. 15-113, Academic Press, San Diego.
    • (1985) The Peptides , vol.7 , pp. 15-113
    • Woody, R.W.1
  • 94
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., Wu, C.-S. C. & Martinez, H. M. (1986). Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.-S.C.2    Martinez, H.M.3
  • 95
    • 0017086768 scopus 로고
    • Near-UV circular dichroism of trypsin inhibitor of adzuki beans attributable to disulfide groups
    • Yoshida, C., Yoshikawa, M. & Takagi, T. (1976). Near-UV circular dichroism of trypsin inhibitor of adzuki beans attributable to disulfide groups. J. Biochem. (Tokyo), 80, 449-454.
    • (1976) J. Biochem. (Tokyo) , vol.80 , pp. 449-454
    • Yoshida, C.1    Yoshikawa, M.2    Takagi, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.