메뉴 건너뛰기




Volumn 50, Issue 29, 2011, Pages 6498-6507

A circumventing role for the non-native intermediate in the folding of β-lactoglobulin

Author keywords

[No Author keywords available]

Indexed keywords

CHARACTERISTIC PROPERTIES; ENERGY LANDSCAPE; FOLDING INTERMEDIATES; FOLDING PATHWAY; FOLDING REACTIONS; HELICAL STRUCTURES; LACTOGLOBULIN; NATIVE FORMS; NON-NATIVE; STOPPED FLOW; WILD TYPES;

EID: 79960507064     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200241a     Document Type: Article
Times cited : (14)

References (55)
  • 1
    • 33846901901 scopus 로고    scopus 로고
    • Intermediates: ubiquitous species on folding energy landscapes?
    • DOI 10.1016/j.sbi.2007.01.003, PII S0959440X07000048, Foldinf and Binding / Protein-Nucleic Interactions
    • Brockwell, D. J. and Radford, S. E. (2007) Intermediates: Ubiquitous species on folding energy landscapes? Curr. Opin. Struct. Biol. 17, 30-37 (Pubitemid 46240814)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.1 , pp. 30-37
    • Brockwell, D.J.1    Radford, S.E.2
  • 2
    • 3342991494 scopus 로고    scopus 로고
    • Experimental investigation of protein folding and misfolding
    • DOI 10.1016/j.ymeth.2004.03.002, PII S1046202304000477
    • Dobson, C. M. (2004) Experimental investigation of protein folding and misfolding Methods 34, 4-14 (Pubitemid 38993205)
    • (2004) Methods , vol.34 , Issue.1 , pp. 4-14
    • Dobson, C.M.1
  • 3
    • 0036183221 scopus 로고    scopus 로고
    • Im7 folding mechanism: Misfolding on a path to the native state
    • DOI 10.1038/nsb757
    • Capaldi, A. P., Kleanthous, C., and Radford, S. E. (2002) Im7 folding mechanism: Misfolding on a path to the native state Nat. Struct. Biol. 9, 209-216 (Pubitemid 34171314)
    • (2002) Nature Structural Biology , vol.9 , Issue.3 , pp. 209-216
    • Capaldi, A.P.1    Kleanthous, C.2    Radford, S.E.3
  • 4
    • 58049200780 scopus 로고    scopus 로고
    • Extensive formation of off-pathway species during folding of an α-β Parallel protein is due to docking of (non)native structure elements in unfolded molecules
    • Nabuurs, S. M., Westphal, A. H., and van Mierlo, C. P. (2008) Extensive formation of off-pathway species during folding of an α-β parallel protein is due to docking of (non)native structure elements in unfolded molecules J. Am. Chem. Soc. 130, 16914-16920
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 16914-16920
    • Nabuurs, S.M.1    Westphal, A.H.2    Van Mierlo, C.P.3
  • 5
    • 57049128788 scopus 로고    scopus 로고
    • Aromatic residues engineered into the β-turn nucleation site of ubiquitin lead to a complex folding landscape, non-native side-chain interactions, and kinetic traps
    • Rea, A. M., Simpson, E. R., Meldrum, J. K., Williams, H. E., and Searle, M. S. (2008) Aromatic residues engineered into the β-turn nucleation site of ubiquitin lead to a complex folding landscape, non-native side-chain interactions, and kinetic traps Biochemistry 47, 12910-12922
    • (2008) Biochemistry , vol.47 , pp. 12910-12922
    • Rea, A.M.1    Simpson, E.R.2    Meldrum, J.K.3    Williams, H.E.4    Searle, M.S.5
  • 7
    • 44449152167 scopus 로고    scopus 로고
    • Disulfide-linked bovine β-lactoglobulin dimers fold slowly, navigating a glassy folding landscape
    • DOI 10.1021/bi8001715
    • Yagi, M., Kameda, A., Sakurai, K., Nishimura, C., and Goto, Y. (2008) Disulfide-linked bovine β-lactoglobulin dimers fold slowly, navigating a glassy folding landscape Biochemistry 47, 5996-6006 (Pubitemid 351770029)
    • (2008) Biochemistry , vol.47 , Issue.22 , pp. 5996-6006
    • Yagi, M.1    Kameda, A.2    Sakurai, K.3    Nishimura, C.4    Goto, Y.5
  • 8
    • 33644954340 scopus 로고    scopus 로고
    • Time-resolved small-angle X-ray scattering investigation of the folding dynamics of heme oxygenase: Implication of the scaling relationship for the submillisecond intermediates of protein folding
    • Uzawa, T., Kimura, T., Ishimori, K., Morishima, I., Matsui, T., Ikeda-Saito, M., Takahashi, S., Akiyama, S., and Fujisawa, T. (2006) Time-resolved small-angle X-ray scattering investigation of the folding dynamics of heme oxygenase: Implication of the scaling relationship for the submillisecond intermediates of protein folding J. Mol. Biol. 357, 997-1008
    • (2006) J. Mol. Biol. , vol.357 , pp. 997-1008
    • Uzawa, T.1    Kimura, T.2    Ishimori, K.3    Morishima, I.4    Matsui, T.5    Ikeda-Saito, M.6    Takahashi, S.7    Akiyama, S.8    Fujisawa, T.9
  • 11
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson, H. J. and Wright, P. E. (2004) Unfolded proteins and protein folding studied by NMR Chem. Rev. 104, 3607-3622
    • (2004) Chem. Rev. , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 12
    • 27144532135 scopus 로고    scopus 로고
    • Solution structure of a protein denatured state and folding intermediate
    • DOI 10.1038/nature04054, PII N04054
    • Religa, T. L., Markson, J. S., Mayor, U., Freund, S. M., and Fersht, A. R. (2005) Solution structure of a protein denatured state and folding intermediate Nature 437, 1053-1056 (Pubitemid 41486989)
    • (2005) Nature , vol.437 , Issue.7061 , pp. 1053-1056
    • Religa, T.L.1    Markson, J.S.2    Mayor, U.3    Freund, S.M.V.4    Fersht, A.R.5
  • 13
    • 11244328062 scopus 로고    scopus 로고
    • Protein folding in high-dimensional spaces: Hypergutters and the role of nonnative interactions
    • DOI 10.1529/biophysj.103.036616
    • McLeish, T. C. (2005) Protein folding in high-dimensional spaces: Hypergutters and the role of nonnative interactions Biophys. J. 88, 172-183 (Pubitemid 40070667)
    • (2005) Biophysical Journal , vol.88 , Issue.1 , pp. 172-183
    • McLeish, T.C.B.1
  • 16
    • 0016209912 scopus 로고
    • Structural principles of the globular organization of protein chains. A stereochemical theory of globular protein secondary structure
    • Lim, V. I. (1974) Structural principles of the globular organization of protein chains. A stereochemical theory of globular protein secondary structure J. Mol. Biol. 88, 857-872
    • (1974) J. Mol. Biol. , vol.88 , pp. 857-872
    • Lim, V.I.1
  • 17
    • 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
  • 18
    • 0034684161 scopus 로고    scopus 로고
    • The core lipocalin, bovine β-lactoglobulin
    • Sawyer, L. and Kontopidis, G. (2000) The core lipocalin, bovine β-lactoglobulin Biochim. Biophys. Acta 1482, 136-148
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 136-148
    • Sawyer, L.1    Kontopidis, G.2
  • 20
    • 0032741871 scopus 로고    scopus 로고
    • Solution structure and dynamics of bovine β-lactoglobulin A
    • Kuwata, K., Hoshino, M., Forge, V., Era, S., Batt, C. A., and Goto, Y. (1999) Solution structure and dynamics of bovine β-lactoglobulin A Protein Sci. 8, 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
  • 21
    • 0039842514 scopus 로고    scopus 로고
    • Structural changes accompanying pH-induced dissociation of the β- lactoglobulin dimer
    • DOI 10.1021/bi992629o
    • Uhrínová, S., Smith, M. H., Jameson, G. B., Uhrín, D., Sawyer, L., and Barlow, P. N. (2000) Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer Biochemistry 39, 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
  • 22
    • 33947316219 scopus 로고    scopus 로고
    • Promiscuous Binding of Ligands by β-Lactoglobulin Involves Hydrophobic Interactions and Plasticity
    • DOI 10.1016/j.jmb.2007.01.077, PII S0022283607001544
    • Konuma, T., Sakurai, K., and Goto, Y. (2007) Promiscuous binding of ligands by β-lactoglobulin involves hydrophobic interactions and plasticity J. Mol. Biol. 368, 209-218 (Pubitemid 46441219)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.1 , pp. 209-218
    • Konuma, T.1    Sakurai, K.2    Goto, Y.3
  • 23
    • 0034769732 scopus 로고    scopus 로고
    • Salt-dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3
    • DOI 10.1110/ps.17001
    • Sakurai, K., Oobatake, M., and Goto, Y. (2001) Salt-dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3 Protein Sci. 10, 2325-2335 (Pubitemid 32988648)
    • (2001) Protein Science , vol.10 , Issue.11 , pp. 2325-2335
    • Sakurai, K.1    Oobatake, M.2    Goto, Y.3
  • 24
    • 0029740071 scopus 로고    scopus 로고
    • Non-native α-helical intermediate in the refolding of β- lactoglobulin, a predominantly β-sheet protein
    • DOI 10.1038/nsb1096-868
    • Hamada, D., Segawa, S., and Goto, Y. (1996) Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein Nat. Struct. Biol. 3, 868-873 (Pubitemid 26330638)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 868-873
    • Hamada, D.1    Segawa, S.-I.2    Goto, Y.3
  • 25
    • 0032491317 scopus 로고    scopus 로고
    • α→β transition of β-lactoglobulin as evidenced by heteronuclear NMR
    • DOI 10.1006/jmbi.1998.2117
    • Kuwata, K., Hoshino, M., Era, S., Batt, C. A., and Goto, Y. (1998) α→β transition of β-lactoglobulin as evidenced by heteronuclear NMR J. Mol. Biol. 283, 731-739 (Pubitemid 28495342)
    • (1998) Journal of Molecular Biology , vol.283 , Issue.4 , pp. 731-739
    • Kuwata, K.1    Hoshino, M.2    Era, S.3    Batt, C.A.4    Goto, Y.5
  • 26
    • 0035150938 scopus 로고    scopus 로고
    • Structural and kinetic characterization of early folding events in β-lactoglobulin
    • DOI 10.1038/84145
    • Kuwata, K., Shastry, R., Cheng, H., Hoshino, M., Batt, C. A., Goto, Y., and Roder, H. (2001) Structural and kinetic characterization of early folding events in β-lactoglobulin Nat. Struct. Biol. 8, 151-155 (Pubitemid 32116068)
    • (2001) Nature Structural Biology , vol.8 , Issue.2 , pp. 151-155
    • Kuwata, K.1    Shastry, R.2    Cheng, H.3    Hoshino, M.4    Batt, C.A.5    Goto, Y.6    Roder, H.7
  • 27
    • 0029588554 scopus 로고
    • High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein
    • DOI 10.1006/jmbi.1995.0651
    • Hamada, D., Kuroda, Y., Tanaka, T., and 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 (Pubitemid 26001804)
    • (1995) Journal of Molecular Biology , vol.254 , Issue.4 , pp. 737-746
    • Hamada, D.1    Kuroda, Y.2    Tanaka, T.3    Goto, Y.4
  • 28
    • 0030334664 scopus 로고    scopus 로고
    • High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy
    • Kuroda, Y., Hamada, D., Tanaka, T., and Goto, Y. (1996) High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy Folding Des. 1, 255-263 (Pubitemid 126748183)
    • (1996) Folding and Design , vol.1 , Issue.4 , pp. 255-263
    • Kuroda, Y.1    Hamada, D.2    Tanaka, T.3    Goto, Y.4
  • 29
    • 0031580203 scopus 로고    scopus 로고
    • The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure
    • DOI 10.1006/jmbi.1997.1055
    • Hamada, D. and Goto, Y. (1997) The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure J. Mol. Biol. 269, 479-487 (Pubitemid 27267862)
    • (1997) Journal of Molecular Biology , vol.269 , Issue.4 , pp. 479-487
    • Hamada, D.1    Goto, Y.2
  • 30
    • 0032498226 scopus 로고    scopus 로고
    • Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy
    • DOI 10.1006/jmbi.1997.1456
    • Arai, M., Ikura, T., Semisotnov, G. V., Kihara, H., Amemiya, Y., and Kuwajima, K. (1998) Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy J. Mol. Biol. 275, 149-162 (Pubitemid 28022394)
    • (1998) Journal of Molecular Biology , vol.275 , Issue.1 , pp. 149-162
    • Arai, M.1    Ikura, T.2    Semisotnov, G.V.3    Kihara, H.4    Amemiya, Y.5    Kuwajima, K.6
  • 31
    • 0344012492 scopus 로고    scopus 로고
    • Reversible Unfolding of Bovine β-Lactoglobulin Mutants without a Free Thiol Group
    • DOI 10.1074/jbc.M308592200
    • Yagi, M., Sakurai, K., Kalidas, C., Batt, C. A., and Goto, Y. (2003) Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group J. Biol. Chem. 278, 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
  • 32
    • 0029843044 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain
    • DOI 10.1021/bi9615699
    • Doering, D. S. and Matsudaira, P. (1996) Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin binding site and structural features of the domain Biochemistry 35, 12677-12685 (Pubitemid 26337322)
    • (1996) Biochemistry , vol.35 , Issue.39 , pp. 12677-12685
    • Doering, D.S.1    Matsudaira, P.2
  • 33
    • 0037067765 scopus 로고    scopus 로고
    • Manipulating monomer-dimer equilibrium of bovine β-lactoglobulin by amino acid substitution
    • DOI 10.1074/jbc.M203659200
    • Sakurai, K. and Goto, Y. (2002) Manipulating monomer-dimer equilibrium of bovine β-lactoglobulin by amino acid substitution J. Biol. Chem. 277, 25735-25740 (Pubitemid 34951894)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25735-25740
    • Sakurai, K.1    Goto, Y.2
  • 34
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S. C. and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182, 319-326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 35
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • DOI 10.1016/0022-2836(84)90309-7
    • Eisenberg, D., Schwarz, E., Komaromy, M., and Wall, R. (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot J. Mol. Biol. 179, 125-142 (Pubitemid 16223392)
    • (1984) Journal of Molecular Biology , vol.179 , Issue.1 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 36
    • 0031736060 scopus 로고    scopus 로고
    • Role of free Cys121 in stabilization of bovine β-lactoglobulin B
    • Burova, T. V., Choiset, Y., Tran, V., and Haertlé, T. (1998) Role of free Cys121 in stabilization of bovine β-lactoglobulin B Protein Eng. 11, 1065-1073 (Pubitemid 28548501)
    • (1998) Protein Engineering , vol.11 , Issue.11 , pp. 1065-1073
    • Burova, T.V.1    Choiset, Y.2    Tran, V.3    Haertle, T.4
  • 37
    • 0021111048 scopus 로고
    • Conformational stability of mixed disulfide derivatives of β-lactoglobulin B
    • Cupo, J. F. and Pace, C. N. (1983) Conformational stability of mixed disulfide derivatives of β-lactoglobulin B Biochemistry 22, 2654-2658
    • (1983) Biochemistry , vol.22 , pp. 2654-2658
    • Cupo, J.F.1    Pace, C.N.2
  • 38
    • 0028180780 scopus 로고
    • Differences in the processes of β-lactoglobulin cold and heat denaturations
    • Griko, Yu. V. and Kutyshenko, V. P. (1994) Differences in the processes of β-lactoglobulin cold and heat denaturations Biophys. J. 67, 356-363
    • (1994) Biophys. J. , vol.67 , pp. 356-363
    • Griko, Yu.V.1    Kutyshenko, V.P.2
  • 39
    • 0033501546 scopus 로고    scopus 로고
    • Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH
    • DOI 10.1016/S0958-6946(99)00148-X, PII S095869469900148X
    • Schokker, E. P., Singh, H., Pinder, D. N., Noriss, 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 (Pubitemid 30147211)
    • (1999) International Dairy Journal , vol.9 , Issue.11 , pp. 791-800
    • Schokker, E.P.1    Singh, H.2    Pinder, D.N.3    Norris, G.E.4    Creamer, L.K.5
  • 40
    • 0034967751 scopus 로고    scopus 로고
    • Conformational characterization of oligomeric intermediates and aggregates in β-lactoglobulin heat aggregation
    • DOI 10.1110/ps.42501
    • 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 (Pubitemid 32568098)
    • (2001) Protein Science , vol.10 , Issue.7 , pp. 1312-1318
    • Carrotta, R.1    Bauer, R.2    Waninge, R.3    Rischel, C.4
  • 41
    • 0037423721 scopus 로고    scopus 로고
    • Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin
    • DOI 10.1016/S0006-291X(02)02997-2
    • Croguennec, T., Bouhallab, S., Mollé, D., OKennedy, B. T., and Mehra, R. (2003) Stable monomeric intermediate with exposed Cys-119 is formed during heat denaturation of β-lactoglobulin Biochem. Biophys. Res. Commun. 301, 465-471 (Pubitemid 36279263)
    • (2003) Biochemical and Biophysical Research Communications , vol.301 , Issue.2 , pp. 465-471
    • Croguennec, T.1    Bouhallab, S.2    Molle, D.3    O'Kennedy, B.T.4    Mehra, R.5
  • 42
    • 0034598947 scopus 로고    scopus 로고
    • Is folding of β-lactoglobulin non-hierarchic? Intermediate with native-like β-sheet and non-native α-helix
    • Forge, V., Hoshino, M., Kuwata, K., Arai, M., Kuwajima, K., Batt, C. A., and Goto, Y. (2000) Is folding of β-lactoglobulin non-hierarchic? Intermediate with native-like β-sheet and non-native α-helix J. Mol. Biol. 296, 1039-1051
    • (2000) J. Mol. Biol. , vol.296 , pp. 1039-1051
    • Forge, V.1    Hoshino, M.2    Kuwata, K.3    Arai, M.4    Kuwajima, K.5    Batt, C.A.6    Goto, Y.7
  • 43
    • 0037176830 scopus 로고    scopus 로고
    • Peptide models of folding initiation sites of bovine β- lactoglobulin: Identification of nativelike hydrophobic interactions involving G and H strands
    • DOI 10.1021/bi011615r
    • Ragona, L., Catalano, M., Zetta, L., Longhi, R., Fogolari, F., and Molinari, H. (2002) Peptide models of folding initiation sites of bovine β-lactoglobulin: Identification of nativelike hydrophobic interactions involving G and H strands Biochemistry 41, 2786-2796 (Pubitemid 34168948)
    • (2002) Biochemistry , vol.41 , Issue.8 , pp. 2786-2796
    • Ragona, L.1    Catalano, M.2    Zetta, L.3    Longhi, R.4    Fogolari, F.5    Molinari, H.6
  • 44
    • 0033527582 scopus 로고    scopus 로고
    • Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements
    • DOI 10.1006/jmbi.1999.3191
    • Ragona, L., Fogolari, F., Romagnoli, S., Zetta, L., Maubois, J. L., and Molinari, H. (1999) Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements J. Mol. Biol. 293, 953-969 (Pubitemid 29527676)
    • (1999) Journal of Molecular Biology , vol.293 , Issue.4 , pp. 953-969
    • Ragona, L.1    Fogolari, F.2    Romagnoli, S.3    Zetta, L.4    Maubois, J.L.5    Molinari, H.6
  • 45
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: Implication for non-hierarchical protein folding
    • Shiraki, K., Nishikawa, K., and 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
  • 46
    • 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., and Nagamura, T. (1987) Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism FEBS Lett. 221, 115-118
    • (1987) FEBS Lett. , vol.221 , pp. 115-118
    • Kuwajima, K.1    Yamaya, H.2    Miwa, S.3    Sugai, S.4    Nagamura, T.5
  • 47
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N. and 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.1    Fasman, G.D.2
  • 48
    • 33747592347 scopus 로고    scopus 로고
    • The experimental survey of protein-folding energy landscapes
    • DOI 10.1017/S0033583506004185, PII S0033583506004185
    • Oliveberg, M. and Wolynes, P. G. (2005) The experimental survey of protein-folding energy landscapes Q. Rev. Biophys. 38, 245-288 (Pubitemid 44268537)
    • (2005) Quarterly Reviews of Biophysics , vol.38 , Issue.3 , pp. 245-288
    • Oliveberg, M.1    Wolynes, P.G.2
  • 49
    • 0033548458 scopus 로고    scopus 로고
    • The Greek key protein apo-pseudoazurin folds through an obligate on-pathway intermediate
    • DOI 10.1006/jmbi.1998.2588
    • Capaldi, A. P., Ferguson, S. J., and Radford, S. E. (1999) The Greek key protein apo-pseudoazurin folds through an obligate on-pathway intermediate J. Mol. Biol. 286, 1621-1632 (Pubitemid 29121739)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.5 , pp. 1621-1632
    • Capaldi, A.P.1    Ferguson, S.J.2    Radford, S.E.3
  • 50
    • 33745965316 scopus 로고    scopus 로고
    • Population of On-pathway Intermediates in the Folding of Ubiquitin
    • DOI 10.1016/j.jmb.2006.05.061, PII S0022283606006760
    • Crespo, M. D., Simpson, E. R., and Searle, M. S. (2006) Population of on-pathway intermediates in the folding of ubiquitin J. Mol. Biol. 360, 1053-1066 (Pubitemid 44062513)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.5 , pp. 1053-1066
    • Crespo, M.D.1    Simpson, E.R.2    Searle, M.S.3
  • 51
    • 0035807845 scopus 로고    scopus 로고
    • Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway
    • DOI 10.1021/bi011500n
    • Cavagnero, S., Nishimura, C., Schwarzinger, S., Dyson, H. J., and Wright, P. E. (2001) Conformational and dynamic characterization of the molten globule state of an apomyoglobin mutant with an altered folding pathway Biochemistry 40, 14459-14467 (Pubitemid 33111728)
    • (2001) Biochemistry , vol.40 , Issue.48 , pp. 14459-14467
    • Cavagnero, S.1    Nishimura, C.2    Schwarzinger, S.3    Dyson, H.J.4    Wright, P.E.5
  • 52
    • 77952913083 scopus 로고    scopus 로고
    • The plastic energy landscape of protein folding: A triangular folding mechanism with an equilibrium intermediate for a small protein domain
    • Haq, S. R., Jurgens, M. C., Chi, C. N., Koh, C. S., Elfstrom, L., Selmer, M., Gianni, S., and Jemth, P. (2010) The plastic energy landscape of protein folding: A triangular folding mechanism with an equilibrium intermediate for a small protein domain J. Biol. Chem. 285, 18051-18059
    • (2010) J. Biol. Chem. , vol.285 , pp. 18051-18059
    • Haq, S.R.1    Jurgens, M.C.2    Chi, C.N.3    Koh, C.S.4    Elfstrom, L.5    Selmer, M.6    Gianni, S.7    Jemth, P.8
  • 54
    • 66249095623 scopus 로고    scopus 로고
    • Non-native α-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and β-lactoglobulin
    • Tsukamoto, S., Yamashita, T., Yamada, Y., Fujiwara, K., Maki, K., Kuwajima, K., Matsumura, Y., Kihara, H., Tsuge, H., and Ikeguchi, M. (2009) Non-native α-helix formation is not necessary for folding of lipocalin: Comparison of burst-phase folding between tear lipocalin and β-lactoglobulin Proteins 76, 226-236
    • (2009) Proteins , vol.76 , pp. 226-236
    • Tsukamoto, S.1    Yamashita, T.2    Yamada, Y.3    Fujiwara, K.4    Maki, K.5    Kuwajima, K.6    Matsumura, Y.7    Kihara, H.8    Tsuge, H.9    Ikeguchi, M.10
  • 55
    • 0035029214 scopus 로고    scopus 로고
    • ANTHEPROT: An integrated protein sequence analysis software with client/server capabilities
    • DOI 10.1016/S0010-4825(01)00008-7, PII S0010482501000087
    • Deléage, G., Combet, C., Blanchet, C., and Geourjon, C. (2001) ANTHEPROT: An integrated protein sequence analysis software with client/server capabilities Comput. Biol. Med. 31, 259-267 (Pubitemid 32378727)
    • (2001) Computers in Biology and Medicine , vol.31 , Issue.4 , pp. 259-267
    • Deleage, G.1    Combet, C.2    Blanchet, C.3    Geourjon, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.