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Volumn 394, Issue 2, 2009, Pages 351-362

The Human α-Lactalbumin Molten Globule: Comparison of Structural Preferences at pH 2 and pH 7

Author keywords

human lactalbumin; molten globule; NMR; pH dependence; protein folding

Indexed keywords

ALPHA LACTALBUMIN; AMINO ACID;

EID: 70350524972     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.09.025     Document Type: Article
Times cited : (37)

References (42)
  • 1
    • 0032539684 scopus 로고    scopus 로고
    • Is the molten globule a third phase of proteins?
    • Pande V.S., and Rokhsar D.S. Is the molten globule a third phase of proteins?. Proc. Natl Acad. Sci. USA 95 (1998) 1490-1494
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1490-1494
    • Pande, V.S.1    Rokhsar, D.S.2
  • 3
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Adv. Protein Chem. 47 (1995) 83-229
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 4
    • 0025938928 scopus 로고
    • Proposed molten globule intermediates in Fd phage penetration and assembly
    • Dunker A.K., Ensign L.D., Arnold G.E., and Roberts L.M. Proposed molten globule intermediates in Fd phage penetration and assembly. FEBS Lett. 292 (1991) 275-278
    • (1991) FEBS Lett. , vol.292 , pp. 275-278
    • Dunker, A.K.1    Ensign, L.D.2    Arnold, G.E.3    Roberts, L.M.4
  • 5
    • 0027406036 scopus 로고
    • Mechanism of pH-induced release of retinol from retinol-binding protein
    • Ptitsyn O.B., Zanotti G., Denesyuk A.L., and Bychkova V.E. Mechanism of pH-induced release of retinol from retinol-binding protein. FEBS Lett. 317 (1993) 181-184
    • (1993) FEBS Lett. , vol.317 , pp. 181-184
    • Ptitsyn, O.B.1    Zanotti, G.2    Denesyuk, A.L.3    Bychkova, V.E.4
  • 6
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson F.M., Wright P.E., and Baldwin R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science 249 (1990) 1544-1548
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 7
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of α-lactalbumin
    • Kuwajima K. The molten globule state of α-lactalbumin. FASEB J. 10 (1996) 102-109
    • (1996) FASEB J. , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 8
    • 0030010408 scopus 로고    scopus 로고
    • Intermediate states in protein folding
    • Privalov P.L. Intermediate states in protein folding. J. Mol. Biol. 258 (1996) 707-725
    • (1996) J. Mol. Biol. , vol.258 , pp. 707-725
    • Privalov, P.L.1
  • 9
    • 0026244229 scopus 로고
    • MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
    • Kraulis P.K. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24 (1991) 946-950
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.K.1
  • 11
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima K. The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins 6 (1989) 87-103
    • (1989) Proteins , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 12
    • 0027536094 scopus 로고
    • Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: a two-dimensional NMR study
    • Alexandrescu A.T., Evans P.A., Pitkeathly M., Baum J., and Dobson C.M. Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: a two-dimensional NMR study. Biochemistry 32 (1993) 1707-1718
    • (1993) Biochemistry , vol.32 , pp. 1707-1718
    • Alexandrescu, A.T.1    Evans, P.A.2    Pitkeathly, M.3    Baum, J.4    Dobson, C.M.5
  • 13
    • 0028334906 scopus 로고
    • A protein dissection study of a molten globule
    • Peng Z.Y., and Kim P.S. A protein dissection study of a molten globule. Biochemistry 33 (1994) 2136-2141
    • (1994) Biochemistry , vol.33 , pp. 2136-2141
    • Peng, Z.Y.1    Kim, P.S.2
  • 14
    • 0028952169 scopus 로고
    • Bipartite structure of the α-lactalbumin molten globule
    • Wu L.C., Peng Z.Y., and Kim P.S. Bipartite structure of the α-lactalbumin molten globule. Nat. Struct. Biol. 2 (1995) 281-286
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 281-286
    • Wu, L.C.1    Peng, Z.Y.2    Kim, P.S.3
  • 15
    • 0030768045 scopus 로고    scopus 로고
    • A residue-specific NMR view of the non-cooperative unfolding of a molten globule
    • Schulman B.A., Kim P.S., Dobson C.M., and Redfield C. A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nat. Struct. Biol. 4 (1997) 630-634
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 16
    • 0029765444 scopus 로고    scopus 로고
    • Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology
    • Schulman B.A., and Kim P.S. Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology. Nat. Struct. Biol. 3 (1996) 682-687
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 682-687
    • Schulman, B.A.1    Kim, P.S.2
  • 17
    • 0028866620 scopus 로고
    • Different subdomains are most protected from hydrogen-exchange in the molten globule and native states of human α-lactalbumin
    • Schulman B.A., Redfield C., Peng Z.Y., Dobson C.M., and Kim P.S. Different subdomains are most protected from hydrogen-exchange in the molten globule and native states of human α-lactalbumin. J. Mol. Biol. 253 (1995) 651-657
    • (1995) J. Mol. Biol. , vol.253 , pp. 651-657
    • Schulman, B.A.1    Redfield, C.2    Peng, Z.Y.3    Dobson, C.M.4    Kim, P.S.5
  • 18
    • 0035943398 scopus 로고    scopus 로고
    • Probing subtle differences in the hydrogen exchange behavior of variants of the human α-lactalbumin molten globule using mass spectrometry
    • Last A.M., Schulman B.A., Robinson C.V., and Redfield C. Probing subtle differences in the hydrogen exchange behavior of variants of the human α-lactalbumin molten globule using mass spectrometry. J. Mol. Biol. 311 (2001) 909-919
    • (2001) J. Mol. Biol. , vol.311 , pp. 909-919
    • Last, A.M.1    Schulman, B.A.2    Robinson, C.V.3    Redfield, C.4
  • 19
    • 0037661368 scopus 로고    scopus 로고
    • pH-dependent stability of the human α-lactalbumin molten globule state: contrasting roles of the 6-120 disulfide and the Δ-subdomain at low and neutral pH
    • Horng J.C., Demarest S.J., and Raleigh D.P. pH-dependent stability of the human α-lactalbumin molten globule state: contrasting roles of the 6-120 disulfide and the Δ-subdomain at low and neutral pH. Proteins: Struct. Funct. Genet. 52 (2003) 193-202
    • (2003) Proteins: Struct. Funct. Genet. , vol.52 , pp. 193-202
    • Horng, J.C.1    Demarest, S.J.2    Raleigh, D.P.3
  • 20
    • 0024533979 scopus 로고
    • Characterization of a partly folded protein by NMR methods-studies on the molten globule state of guinea-pig α-lactalbumin
    • Baum J., Dobson C.M., Evans P.A., and Hanley C. Characterization of a partly folded protein by NMR methods-studies on the molten globule state of guinea-pig α-lactalbumin. Biochemistry 28 (1989) 7-13
    • (1989) Biochemistry , vol.28 , pp. 7-13
    • Baum, J.1    Dobson, C.M.2    Evans, P.A.3    Hanley, C.4
  • 23
    • 0033607727 scopus 로고    scopus 로고
    • Characterization of millisecond time-scale dynamics in the molten globule state of α-lactalbumin by NMR
    • Kim S., Bracken C., and Baum J. Characterization of millisecond time-scale dynamics in the molten globule state of α-lactalbumin by NMR. J. Mol. Biol. 294 (1999) 551-560
    • (1999) J. Mol. Biol. , vol.294 , pp. 551-560
    • Kim, S.1    Bracken, C.2    Baum, J.3
  • 24
    • 0028916267 scopus 로고
    • Local structural preferences in the α-lactalbumin molten globule
    • Peng Z.Y., Wu L.C., and Kim P.S. Local structural preferences in the α-lactalbumin molten globule. Biochemistry 34 (1995) 3248-3252
    • (1995) Biochemistry , vol.34 , pp. 3248-3252
    • Peng, Z.Y.1    Wu, L.C.2    Kim, P.S.3
  • 25
    • 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 (1986) 18-27
    • (1986) Int. J. Pept. Protein Res. , vol.27 , pp. 18-27
    • Kuwajima, K.1    Harushima, Y.2    Sugai, S.3
  • 26
    • 0034687724 scopus 로고    scopus 로고
    • Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human α-lactalbumin by circular dichroism spectroscopy
    • Chaudhuri T.K., Arai M., Terada T.P., Ikura T., and Kuwajima K. Equilibrium and kinetic studies on folding of the authentic and recombinant forms of human α-lactalbumin by circular dichroism spectroscopy. Biochemistry 39 (2000) 15643-15651
    • (2000) Biochemistry , vol.39 , pp. 15643-15651
    • Chaudhuri, T.K.1    Arai, M.2    Terada, T.P.3    Ikura, T.4    Kuwajima, K.5
  • 27
    • 0030025082 scopus 로고    scopus 로고
    • Disulfide determinants of calcium-induced packing in α-lactalbumin
    • Wu L.C., Schulman B.A., Peng Z.Y., and Kim P.S. Disulfide determinants of calcium-induced packing in α-lactalbumin. Biochemistry 35 (1996) 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
  • 28
    • 0030993346 scopus 로고    scopus 로고
    • Calcium binding peptides from α-lactalbumin: implications for protein folding and stability
    • Kuhlman B., Boice J.A., Wu W.J., Fairman R., and Raleigh D.P. Calcium binding peptides from α-lactalbumin: implications for protein folding and stability. Biochemistry 36 (1997) 4607-4615
    • (1997) Biochemistry , vol.36 , pp. 4607-4615
    • Kuhlman, B.1    Boice, J.A.2    Wu, W.J.3    Fairman, R.4    Raleigh, D.P.5
  • 29
    • 0032479326 scopus 로고    scopus 로고
    • Contribution of individual residues to formation of the native-like tertiary topology in the α-lactalbumin molten globule
    • Song J., Bai P., Luo L., and Peng Z.Y. Contribution of individual residues to formation of the native-like tertiary topology in the α-lactalbumin molten globule. J. Mol. Biol. 280 (1998) 167-174
    • (1998) J. Mol. Biol. , vol.280 , pp. 167-174
    • Song, J.1    Bai, P.2    Luo, L.3    Peng, Z.Y.4
  • 30
    • 0032479440 scopus 로고    scopus 로고
    • A specific hydrophobic core in the α-lactalbumin molten globule
    • Wu L.C., and Kim P.S. A specific hydrophobic core in the α-lactalbumin molten globule. J. Mol. Biol. 280 (1998) 175-182
    • (1998) J. Mol. Biol. , vol.280 , pp. 175-182
    • Wu, L.C.1    Kim, P.S.2
  • 31
    • 0023041667 scopus 로고
    • Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of α-lactalbumin and lysozyme
    • Ikeguchi M., Kuwajima K., Mitani M., and Sugai S. Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of α-lactalbumin and lysozyme. Biochemistry 25 (1986) 6965-6972
    • (1986) Biochemistry , vol.25 , pp. 6965-6972
    • Ikeguchi, M.1    Kuwajima, K.2    Mitani, M.3    Sugai, S.4
  • 32
    • 0030348041 scopus 로고    scopus 로고
    • Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
    • Arai M., and Kuwajima K. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Folding Des. 1 (1996) 275-287
    • (1996) Folding Des. , vol.1 , pp. 275-287
    • Arai, M.1    Kuwajima, K.2
  • 33
    • 0036349865 scopus 로고    scopus 로고
    • Fast compaction of α- lactalbumin during folding studied by stopped-flow X-ray scattering
    • Arai M., Ito K., Inobe T., Nakao M., Maki K., Kamagata K., et al. Fast compaction of α- lactalbumin during folding studied by stopped-flow X-ray scattering. J. Mol. Biol. 321 (2002) 121-132
    • (2002) J. Mol. Biol. , vol.321 , pp. 121-132
    • Arai, M.1    Ito, K.2    Inobe, T.3    Nakao, M.4    Maki, K.5    Kamagata, K.6
  • 34
    • 16544381119 scopus 로고    scopus 로고
    • Conformation-dependent interaction of α-lactalbumin with model and biological membranes: a spin-label ESR study
    • Chaudhuri D., Narayan M., and Berliner L.J. Conformation-dependent interaction of α-lactalbumin with model and biological membranes: a spin-label ESR study. Protein J. 23 (2004) 95-101
    • (2004) Protein J. , vol.23 , pp. 95-101
    • Chaudhuri, D.1    Narayan, M.2    Berliner, L.J.3
  • 36
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings P.A., and Wright P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262 (1993) 892-896
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 37
    • 0030473296 scopus 로고    scopus 로고
    • Kinetic intermediates in the formation of the cytochrome c molten globule
    • Colon W., and Roder H. Kinetic intermediates in the formation of the cytochrome c molten globule. Nat. Struct. Biol. 3 (1996) 1019-1025
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 1019-1025
    • Colon, W.1    Roder, H.2
  • 38
    • 67149118906 scopus 로고    scopus 로고
    • Early events, kinetic intermediates and the mechanism of protein folding in cytochrome c
    • Goldbeck R.A., Chen E., and Kliger D.S. Early events, kinetic intermediates and the mechanism of protein folding in cytochrome c. Int. J. Mol. Sci. 10 (2009) 1476-1499
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 1476-1499
    • Goldbeck, R.A.1    Chen, E.2    Kliger, D.S.3
  • 39
    • 0029598779 scopus 로고
    • Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study
    • Yamasaki K., Ogasahara K., Yutani K., Oobatake M., and Kanaya S. Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism, fluorescence, and NMR study. Biochemistry 34 (1995) 16552-16562
    • (1995) Biochemistry , vol.34 , pp. 16552-16562
    • Yamasaki, K.1    Ogasahara, K.2    Yutani, K.3    Oobatake, M.4    Kanaya, S.5
  • 40
    • 0029811784 scopus 로고    scopus 로고
    • Structure of the acid state of Escherichia coli ribonuclease HI
    • Dabora J.M., Pelton J.G., and Marqusee S. Structure of the acid state of Escherichia coli ribonuclease HI. Biochemistry 35 (1996) 11951-11958
    • (1996) Biochemistry , vol.35 , pp. 11951-11958
    • Dabora, J.M.1    Pelton, J.G.2    Marqusee, S.3
  • 41
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L.E., Keifer P., and Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114 (1992) 10663-10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 42
    • 0025210153 scopus 로고
    • Complete resonance assignment for the polypeptide backbone of interleukin 1 Δ using three-dimensional heteronuclear NMR spectroscopy
    • Driscoll P.C., Clore G.M., Marion D., Wingfield P.T., and Gronenborn A.M. Complete resonance assignment for the polypeptide backbone of interleukin 1 Δ using three-dimensional heteronuclear NMR spectroscopy. Biochemistry 29 (1990) 3542-3556
    • (1990) Biochemistry , vol.29 , pp. 3542-3556
    • Driscoll, P.C.1    Clore, G.M.2    Marion, D.3    Wingfield, P.T.4    Gronenborn, A.M.5


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