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Volumn 109, Issue , 2012, Pages 50-57

Tryptophan dynamics in the exploration of micro-conformational changes of refolded β-lactoglobulin after thermal exposure: A steady state and time-resolved fluorescence approach

Author keywords

lg; Dynamics; Intermediates; Lifetime; Refolding; Tryptophan

Indexed keywords

BETA LACTOGLOBULIN; TRYPTOPHAN;

EID: 84858155181     PISSN: 10111344     EISSN: 18732682     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2012.01.005     Document Type: Article
Times cited : (39)

References (51)
  • 2
    • 13544263199 scopus 로고    scopus 로고
    • Epitope mapping of a monoclonal antibody specific to bovine dry milk: Involvement of residues 66-76 of strand D in thermal denatured β-Lactoglobulin
    • DOI 10.1074/jbc.M407031200
    • C.Y. Song, W.L. Chen, M.C. Yang, J.P. Huang, and S.J.T. Mao Epitope mapping of a monoclonal antibody specific to bovine dry milk: involvement of residues 66-76 of β-strand D in thermal denatured β-lactoglobulin J. Biol. Chem. 280 2005 3574 3582 (Pubitemid 40223823)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3574-3582
    • Chun, Y.S.1    Wen, L.C.2    Ming, C.Y.3    Jen, P.H.4    Mao, S.J.T.5
  • 3
    • 0010910801 scopus 로고
    • Detection of conformational modifications of heated β-lactoglobulin by immunochemical methods
    • A. Lalignant, J. Marti, J.C. Cheftel, E. Dumay, and J.C. Cuq Detection of conformational modifications of heated β-lactoglobulin by immunochemical methods J. Agric. Food Chem. 43 1995 2896 2903
    • (1995) J. Agric. Food Chem. , vol.43 , pp. 2896-2903
    • Lalignant, A.1    Marti, J.2    Cheftel, J.C.3    Dumay, E.4    Cuq, J.C.5
  • 4
    • 20844448930 scopus 로고    scopus 로고
    • Structural changes of β-lactoglobulin during thermal unfolding and refolding - An FT-IR and circular dichroism study
    • DOI 10.1007/s10930-004-0603-z
    • C. Bhattacharjee, S. Saha, A. Biswas, M. Kundu, L. Ghosh, and K.P. Das Structural changes of β-lactoglobulin during thermal unfolding and refolding - an FT-IR and circular dichroism study Prot. J. 24 2005 27 35 (Pubitemid 40933100)
    • (2005) Protein Journal , vol.24 , Issue.1 , pp. 27-35
    • Bhattacharjee, C.1    Saha, S.2    Biswas, A.3    Kundu, M.4    Ghosh, L.5    Das, K.P.6
  • 5
    • 0344012492 scopus 로고    scopus 로고
    • Reversible Unfolding of Bovine β-Lactoglobulin Mutants without a Free Thiol Group
    • DOI 10.1074/jbc.M308592200
    • M. Yagi, K. Sakurai, C. Kalidas, A.C. Batt, and Y. Goto Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group J. Biol. Chem. 278 2003 47009 47015 (Pubitemid 37452284)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 47009-47015
    • Yagi, M.1    Sakurai, K.2    Kalidas, C.3    Batt, C.A.4    Goto, Y.5
  • 6
    • 0033922354 scopus 로고    scopus 로고
    • Thermal unfolding and refolding of β-lactoglobulin. An intrinsic and extrinsic fluorescence study
    • DOI 10.1046/j.1432-1327.2000.01409.x
    • C. Bhattacharjee, and K.P. Das Thermal unfolding and refolding of β-lactoglobulin: an intrinsic and extrinsic fluorescence study Eur. J. Biochem. 267 2000 3957 3964 (Pubitemid 30436086)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.13 , pp. 3957-3964
    • Bhattacharjee, C.1    Das, K.P.2
  • 8
    • 62449341938 scopus 로고    scopus 로고
    • Urea but not Guanidinium destabilizes proteins by forming hydrogen bonds to the peptide group
    • W.K. Lim, J. Rosgen, and S.W. Englander Urea but not Guanidinium destabilizes proteins by forming hydrogen bonds to the peptide group Proc. Nat. Acad. Sci. 106 2009 2595 2600
    • (2009) Proc. Nat. Acad. Sci. , vol.106 , pp. 2595-2600
    • Lim, W.K.1    Rosgen, J.2    Englander, S.W.3
  • 9
    • 33947408769 scopus 로고    scopus 로고
    • Guanidinium chloride and urea denaturations of β-Lactoglobulin A at pH 2.0 and 25°C: The equilibrium intermediate contains non-native structures (helix, tryptophan and hydrophobic patches)
    • DOI 10.1016/j.bpc.2007.01.006, PII S0301462207000178
    • T.A. Dar, L.J. Singh, A. Islam, F. Anjum, A.A.M. Mohavedi, and F. Ahmed Guanidinium chloride and urea denaturations of β-lactoglobulin A at 2.0 and 25 °C: the equilibrium intermediate contains non-native structures (helix, tryptophan and hydrophobic patches) Biophys. Chem. 127 2007 140 148 (Pubitemid 46454351)
    • (2007) Biophysical Chemistry , vol.127 , Issue.3 , pp. 140-148
    • Dar, T.A.1    Singh, L.R.2    Islam, A.3    Anjum, F.4    Moosavi-Movahedi, A.A.5    Ahmad, F.6
  • 10
    • 0017230911 scopus 로고
    • The interaction between β-lactoglobulin and sodium n-dodecyl sulphate
    • M.N. Jones, and A. Wilkinson The interaction between β-lactoglobulin and sodium n-dodecyl sulphate Biochem. J. 153 1976 713 718
    • (1976) Biochem. J. , vol.153 , pp. 713-718
    • Jones, M.N.1    Wilkinson, A.2
  • 11
    • 17144407576 scopus 로고    scopus 로고
    • Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of β-lactoglobulin B
    • T. Considine, H.A. Patel, H. Singh, and L.K. Creamer Influence of binding of sodium dodecyl sulfate, all-trans retinol, palmitate and 8-anilino-1-napthalene sulfonate on heat induced unfolding and aggregation of β-lactoglobulin B J. Agric. Food Chem. 53 2005 3197 3205 (Pubitemid 40525286)
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.8 , pp. 3197-3205
    • Considine, T.1    Patel, H.A.2    Singh, H.3    Creamer, L.K.4
  • 12
    • 0027381391 scopus 로고
    • Unfolding/refolding studies on bovine β-lactoglobulin with monoclonal antibodies as probes. Does a renatured protein completely refold?
    • M. Hattori, A. Ametani, Y. Katakura, M. Shimizu, and S. Kaminogawa Unfolding/refolding studies on bovine β-lactoglobulin with monoclonal antibodies as probes J. Biol. Chem. 268 1993 22414 22419 (Pubitemid 23318289)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.30 , pp. 22414-22419
    • Hattori, M.1    Ametani, A.2    Katakura, Y.3    Shimizu, M.4    Kaminogawa, S.5
  • 13
    • 0029911537 scopus 로고    scopus 로고
    • In vitro renaturation of bovine β-lactoglobulin A leads to a biologically active but incompletely refolded state
    • V. Subramaniam, D. Steel, and A. Gafni In vitro renaturation of bovine β-lactoglobulin A leads to a biologically active but incompletely refolded state Prot. Sci. 5 1996 2089 2094 (Pubitemid 26347744)
    • (1996) Protein Science , vol.5 , Issue.10 , pp. 2089-2094
    • Subramaniam, V.1    Steel, D.G.2    Gafni, A.3
  • 14
    • 34848912277 scopus 로고    scopus 로고
    • Principal component analysis of the pH dependent conformational transitions of bovine β-lactoglobulin monitored by heteronuclear NMR
    • K. Sakurai, and Y. Goto Principal component analysis of the pH dependent conformational transitions of bovine β-lactoglobulin monitored by heteronuclear NMR Proc. Nat. Acad. Sci. 104 2007 15346 15352
    • (2007) Proc. Nat. Acad. Sci. , vol.104 , pp. 15346-15352
    • Sakurai, K.1    Goto, Y.2
  • 15
    • 34447341183 scopus 로고    scopus 로고
    • Unfolding and refolding of β-lactoglobulin subjected to high hydrostatic pressure at different pH values and temperatures and its influence on proteolysis
    • DOI 10.1021/jf070170w
    • J. Belloque, R. Chicon, and L.R. Fandino Unfolding and refolding of β-lactoglobulin subjected to high hydrostatic pressure at different pH values and temperatures and its influence on proteolysis J. Agric. Food Chem. 55 2007 5282 5288 (Pubitemid 47056088)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.13 , pp. 5282-5288
    • Belloque, J.1    Chicon, R.2    Lopez-Fandino, R.3
  • 16
    • 0021876620 scopus 로고
    • Homology of β-lactoglobulin, serum retinol-binding protein, and protein HC
    • S. Pervaiz, and K. Brew Homology of β-lactoglobulin, serum retinol-binding protein, and protein HC Science 228 1985 335 337 (Pubitemid 15076832)
    • (1985) Science , vol.228 , Issue.4697 , pp. 335-337
    • Pervaiz, S.1    Brew, K.2
  • 18
    • 0032491188 scopus 로고    scopus 로고
    • Structural basis of the tanford transition of bovine β-lactoglobulin
    • DOI 10.1021/bi981016t
    • B.Y. Qin, M.C. Bewley, L.K. Creamer, H.M. Baker, E.N. Baker, and G.B. Jameson Structural basis of the Tanford transition of bovine β-lactoglobulin Biochemistry 37 1998 14014 14023 (Pubitemid 28471234)
    • (1998) Biochemistry , vol.37 , Issue.40 , pp. 14014-14023
    • Qin, B.Y.1    Bewley, M.C.2    Creamer, L.K.3    Baker, H.M.4    Baker, E.N.5    Jameson, G.B.6
  • 19
    • 0031738305 scopus 로고    scopus 로고
    • 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin
    • DOI 10.1016/S0014-5793(98)01199-5, PII S0014579398011995
    • B.Y. Qin, L.K. Creamer, E.N. Baker, and G.B. Jameson 12- Bromododecanoicacid binds inside the calyx of bovine β-lactoglobulin FEBS Lett. 438 1998 272 278 (Pubitemid 28529288)
    • (1998) FEBS Letters , vol.438 , Issue.3 , pp. 272-278
    • Qin, B.Y.1    Creamer, L.K.2    Baker, E.N.3    Jameson, G.B.4
  • 20
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 resolution
    • H.L. Monaco, G. Zanotti, P. Spadon, M. Bolognesi, L. Sawyer, and E.E. Eliopulos Crystal structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 resolution J. Mol. Biol. 197 1987 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    Eliopulos, E.E.6
  • 21
    • 0032741871 scopus 로고    scopus 로고
    • Solution structure and dynamics of bovine β-lactoglobulin A
    • K. Kuwata, M. Hoshino, V. Forge, S. Era, C.A. Batt, and Y. Goto Solution structure and dynamics of bovine β-lactoglobulin A Prot. Sci. 8 1999 2541 2545 (Pubitemid 29536426)
    • (1999) Protein Science , vol.8 , Issue.11 , pp. 2541-2545
    • Kuwata, K.1    Hoshino, M.2    Forge, V.3    Era, S.4    Batt, C.A.5    Goto, Y.6
  • 22
    • 0032475891 scopus 로고    scopus 로고
    • Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2
    • DOI 10.1016/S0014-5793(98)00936-3, PII S0014579398009363
    • F. Fogolari, L. Ragona, L. Zetta, S. Romagnoli, K.G. DeKruif, and H. Molinari Monomeric bovine β lactoglobulin adopts a β-barrel fold at pH 2 FEBS Lett. 436 1998 149 154 (Pubitemid 28468545)
    • (1998) FEBS Letters , vol.436 , Issue.2 , pp. 149-154
    • Fogolari, F.1    Ragona, L.2    Zetta, L.3    Romagnoli, S.4    De Kruif, K.G.5    Molinari, H.6
  • 23
    • 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 NMR chemical shifts for bovine β-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form J. Biomol. 12 1998 89 107 (Pubitemid 128512836)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.1 , pp. 89-107
    • Uhrinova, S.1    Uhrin, D.2    Denton, H.3    Smith, M.4    Sawyer, L.5    Barlow, P.N.6
  • 24
    • 67349093283 scopus 로고    scopus 로고
    • Structural dynamics and folding of β-lactoglobulin probed by heteronuclear NMR
    • K. Sakurai, T. Konuma, M. Yagi, and Y. Goto Structural dynamics and folding of β-lactoglobulin probed by heteronuclear NMR Biochim. Biophys. Acta 1790 2009 527 537
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 527-537
    • Sakurai, K.1    Konuma, T.2    Yagi, M.3    Goto, Y.4
  • 25
    • 0031875535 scopus 로고    scopus 로고
    • Some aspects of β-lactoglobulin structural properties in solution studied by fluorescence quenching
    • DOI 10.1016/S0141-8130(98)00037-3, PII S0141813098000373
    • P. Busti, C.A. Gatti, and N.J. Delorenzi Some aspects of β-lactoglobulin structural properties in solution studied by fluorescence quenching Int. J. Biol. Macromol. 23 1998 143 148 (Pubitemid 28396141)
    • (1998) International Journal of Biological Macromolecules , vol.23 , Issue.2 , pp. 143-148
    • Busti, P.1    Gatti, C.A.2    Delorenzi, N.J.3
  • 26
    • 30744452464 scopus 로고    scopus 로고
    • Anomalous "unquenching" of the fluorescence decay times of β-lactoglobulin induced by the known quencher acrylamide
    • DOI 10.1016/j.jphotobiol.2005.09.003, PII S1011134405001776
    • C.A. Portugal, J.G. Crespo, and J.C. Lima Anomalous quenching of the fluorescence decay times of beta-lactoglobulin induced by the known quencher acrylamide J. Photochem. Photobiol. B 82 2006 117 126 (Pubitemid 43091809)
    • (2006) Journal of Photochemistry and Photobiology B: Biology , vol.82 , Issue.2 , pp. 117-126
    • Portugal, C.A.M.1    Crespo, J.G.2    Lima, J.C.3
  • 27
    • 0039842514 scopus 로고    scopus 로고
    • Structural changes accompanying pH-induced dissociation of the β- lactoglobulin dimer
    • DOI 10.1021/bi992629o
    • S. Uhrinova, M. Smith, G.B. Jameson, D. Uhrin, L. Sawyer, and P.N. Brownlow Structural changes accompanying pH induced dissociation of β-lactoglobulin dimmer Biochemistry 39 2000 3565 3574 (Pubitemid 30183837)
    • (2000) Biochemistry , vol.39 , Issue.13 , pp. 3565-3574
    • Uhrinova, S.1    Smith, M.H.2    Jameson, G.B.3    Uhrin, D.4    Sawyer, L.5    Barlow, P.N.6
  • 28
    • 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
    • X.L. Qi, C. Holt, D. Mcnulty, D.T. Clarke, S. Brownlow, and G.R. Jones Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of molten globule hypothesis Biochem. J. 324 1997 341 346 (Pubitemid 27229401)
    • (1997) Biochemical Journal , vol.324 , Issue.1 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    Mcnulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 29
    • 20844436321 scopus 로고    scopus 로고
    • β-lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroic spectra
    • W.L. Chen, M.T. Huang, C.Y. Liau, J.C. Ho, K.C. Hong, and S.J.T. Mao β-Lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroism spectra J. Dairy Sci. 88 2005 1618 1630 (Pubitemid 41431211)
    • (2005) Journal of Dairy Science , vol.88 , Issue.5 , pp. 1618-1630
    • Chen, W.L.1    Hwang, M.T.2    Liau, C.Y.3    Ho, J.C.4    Hong, K.C.5    Mao, S.J.T.6
  • 30
    • 15744402967 scopus 로고    scopus 로고
    • Thermal unfolding of bovine β-lactoglobulin studied by UV spectroscopy and fluorescence quenching
    • DOI 10.1016/j.foodres.2004.11.007, PII S0963996904002686
    • P. Busti, C.A. Gatti, and N.J. Delorenzi Thermal unfolding of bovine-lactoglobulin studied by UV-spectroscopy and fluorescence quenching Food Res. Int. 38 2005 543 550 (Pubitemid 40406298)
    • (2005) Food Research International , vol.38 , Issue.5 , pp. 543-550
    • Busti, P.1    Gatti, C.A.2    Delorenzi, N.J.3
  • 31
    • 54049088472 scopus 로고    scopus 로고
    • Loss of structural integrity and hydrophobic ligand binding capacity of acetylated and succinylated bovine β-lactoglobulin
    • J. Chakraborty, N. Das, K.P. Das, and U.C. Halder Loss of structural integrity and hydrophobic ligand binding capacity of acetylated and succinylated bovine β-lactoglobulin Int. Dairy J. 19 2009 43 49
    • (2009) Int. Dairy J. , vol.19 , pp. 43-49
    • Chakraborty, J.1    Das, N.2    Das, K.P.3    Halder, U.C.4
  • 33
    • 78650907815 scopus 로고    scopus 로고
    • Unfolding diminishes fluorescence resonance energy transfer (FRET) of lysine modified β-lactoglobulin: Relevance towards anti-HIV binding
    • J. Chakraborty, N. Das, and U.C. Halder Unfolding diminishes fluorescence resonance energy transfer (FRET) of lysine modified β-lactoglobulin: relevance towards anti-HIV binding J. Photochem. Photobiol. B: Biol. 102 2011 1 10
    • (2011) J. Photochem. Photobiol. B: Biol. , vol.102 , pp. 1-10
    • Chakraborty, J.1    Das, N.2    Halder, U.C.3
  • 34
    • 0020763601 scopus 로고
    • On the origin of non exponential fluorescence decay of tryptophan and its derivatives
    • J.W. Petrich, M.C. Chang, D.B. McDonald, and G.R. Fleming On the origin of non exponential fluorescence decay of tryptophan and its derivatives J. Am. Chem. Soc. 105 1983 3824
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3824
    • Petrich, J.W.1    Chang, M.C.2    McDonald, D.B.3    Fleming, G.R.4
  • 35
    • 68549118866 scopus 로고    scopus 로고
    • Considerations for the construction of the solvation correlation function and implications for the interpretation of dielectric relaxation in proteins
    • S. Bose, R. Adhikary, P. Mukherjee, X. Song, and J.W. Petrich Considerations for the construction of the solvation correlation function and implications for the interpretation of dielectric relaxation in proteins J. Phys. Chem. B 113 2009 11061 11068
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11061-11068
    • Bose, S.1    Adhikary, R.2    Mukherjee, P.3    Song, X.4    Petrich, J.W.5
  • 36
    • 77953744655 scopus 로고    scopus 로고
    • Enzyme catalyzed hydrolysis of cellulose in ionic liquids: A green approach towards the production of biofuels
    • S. Bose, D.W. Armstrong, and J.W. Petrich Enzyme catalyzed hydrolysis of cellulose in ionic liquids: a green approach towards the production of biofuels J. Phys. Chem. B 114 2010 8221 8227
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8221-8227
    • Bose, S.1    Armstrong, D.W.2    Petrich, J.W.3
  • 37
    • 0042427115 scopus 로고
    • Nonexponential fluorescence decay in tryptophan and tryptophan-containing peptides and proteins
    • J.W. Petrich, M.C. Chang, and G.R. Fleming Nonexponential fluorescence decay in tryptophan and tryptophan-containing peptides and proteins NATO ASI Ser., Ser. A 85 1985 77 80
    • (1985) NATO ASI Ser., Ser. A , vol.85 , pp. 77-80
    • Petrich, J.W.1    Chang, M.C.2    Fleming, G.R.3
  • 38
    • 33750927821 scopus 로고
    • Fluorescence decay of tryptophan conformers in aqueous solution
    • A.G. Szabo, and D.M. Rayner Fluorescence decay of tryptophan conformers in aqueous solution J. Am. Chem. Soc. 102 1980 554
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 554
    • Szabo, A.G.1    Rayner, D.M.2
  • 39
    • 0020825202 scopus 로고
    • Quenching-resolved emission anisotropy studies with single and multitryptophan-containing proteins
    • M. Eftink Quenching-resolved emission anisotropy studies with single and multitryptophan-containing proteins Biophys. J. 43 1983 323 334
    • (1983) Biophys. J. , vol.43 , pp. 323-334
    • Eftink, M.1
  • 40
    • 0035290424 scopus 로고    scopus 로고
    • Mild isolation procedure discloses new protein structural properties of β-lactoglobulin
    • H.H.J. de Jongh, T. Groneveld, and J. de Groot Mild isolation procedure discloses new protein structural properties of β-lactoglobulin J. Dairy Sci. 84 2001 562 571 (Pubitemid 33609639)
    • (2001) Journal of Dairy Science , vol.84 , Issue.3 , pp. 562-571
    • De Jongh, H.H.J.1    Groneveld, T.2    De Groot, J.3
  • 41
    • 0000008540 scopus 로고    scopus 로고
    • Thermal Unfolding of β-Lactoglobulin: Characterization of Initial Unfolding Events Responsible for Heat-Induced Aggregation
    • S. Prabhakaran, and S. Damodaran Thermal unfolding of β-lactoglobulin: characterisation of initial unfolding events responsible for heat-induced aggregation J. Agric. Food Chem. 45 1997 4303 4308 (Pubitemid 127491624)
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , Issue.11 , pp. 4303-4308
    • Prabakaran, S.1    Damodaran, S.2
  • 42
    • 11144317965 scopus 로고    scopus 로고
    • Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin
    • DOI 10.1016/j.bpc.2004.07.042, PII S0301462204002108
    • V. Vetri, and V. Militelo Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin Biophys. Chem. 113 2005 83 91 (Pubitemid 40029722)
    • (2005) Biophysical Chemistry , vol.113 , Issue.1 , pp. 83-91
    • Vetri, V.1    Militello, V.2
  • 44
    • 0021114569 scopus 로고
    • Molten-globule state: A compact form of globular proteins with mobile side side-chains
    • M. Ohgushi, and A. Wada Molten-globule state: a compact form of globular proteins with mobile side side-chains FEBS Lett. 164 1983 21 24
    • (1983) FEBS Lett. , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 45
    • 77956178699 scopus 로고    scopus 로고
    • Exploring tryptophan dynamics in acid-induced molten globule state of α-lactalbumin: A wavelength-selective fluorescence approach
    • D.A. Kelkar, A. Chaudhuri, S. Haldar, and A. Chattopadhyay Exploring tryptophan dynamics in acid-induced molten globule state of α-lactalbumin: a wavelength-selective fluorescence approach Eur. Biophys. J. 39 2010 1453 1463
    • (2010) Eur. Biophys. J. , vol.39 , pp. 1453-1463
    • Kelkar, D.A.1    Chaudhuri, A.2    Haldar, S.3    Chattopadhyay, A.4
  • 46
    • 0028180780 scopus 로고
    • Difference in the process of β-lactoglobulin cold and heat denaturation
    • Y.V. Grico, and V.P. Kutyshenko Difference in the process of β-lactoglobulin cold and heat denaturation Biophys. J. 67 1994 356 363
    • (1994) Biophys. J. , vol.67 , pp. 356-363
    • Grico, Y.V.1    Kutyshenko, V.P.2
  • 47
    • 0033810124 scopus 로고    scopus 로고
    • Conformation and stability of thiol-modified bovine β-lactoglobulin
    • K. Sakai, K. Sakurai, M. Sakai, M. Hoshino, and Y. Goto Conformation and stability of thiol-modified bovine β-lactoglobulin Prot. Sci. 9 2000 1719 1729
    • (2000) Prot. Sci. , vol.9 , pp. 1719-1729
    • Sakai, K.1    Sakurai, K.2    Sakai, M.3    Hoshino, M.4    Goto, Y.5
  • 48
    • 79952512858 scopus 로고    scopus 로고
    • Protein misfolding and inclusion body resolubilization
    • G. Chakshumathi, and R. Varadarajan Protein misfolding and inclusion body resolubilization PINSA 68 2002 375 384
    • (2002) PINSA , vol.68 , pp. 375-384
    • Chakshumathi, G.1    Varadarajan, R.2
  • 49
    • 35148874214 scopus 로고    scopus 로고
    • Hydration in protein folding: Thermal unfolding/refolding of human serum albumin
    • DOI 10.1021/la7014447
    • R.K. Mishra, S.S. Sinha, and S.K. Pal Hydration in protein folding: thermal unfolding and refolding of human serum albumin Langmuir 23 2007 10224 10229 (Pubitemid 47548507)
    • (2007) Langmuir , vol.23 , Issue.20 , pp. 10224-10229
    • Mitra, R.K.1    Sinha, S.S.2    Pal, S.K.3
  • 50
    • 35348897426 scopus 로고    scopus 로고
    • Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases
    • DOI 10.1021/bi700754q
    • E. Graczer, A. Varga, I. Hajdu, B. Melnik, A. Szilagyi, G. Semisotnov, P. Zavodszky, and M. Vas Rates of unfolding, rather than refolding, determine thermal stabilities of thermophilic, mesophilic, and psychrotrophic 3-isopropylmalate dehydrogenases Biochemistry 46 2007 11536 11549 (Pubitemid 47585499)
    • (2007) Biochemistry , vol.46 , Issue.41 , pp. 11536-11549
    • Graczer, E.1    Varga, A.2    Hajdu, I.3    Melnik, B.4    Szilagyi, A.5    Semisotnov, G.6    Zavodszky, P.7    Vas, M.8
  • 51
    • 84857641635 scopus 로고    scopus 로고
    • Thermal unfolding and refolding of protein under osmotic pressure clarified by wide-angle X-ray scattering
    • doi: 10. 1016/j.tca.2011.11.019
    • M. Hirai Thermal unfolding and refolding of protein under osmotic pressure clarified by wide-angle X-ray scattering Thermochim. Acta 2011 doi: 10. 1016/j.tca.2011.11.019
    • (2011) Thermochim. Acta
    • Hirai, M.1


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