메뉴 건너뛰기




Volumn 338, Issue 1, 2004, Pages 149-158

Local and global cooperativity in the human α-lactalbumin molten globule

Author keywords

4 SS LA, LA containing the four native disulfide bonds; Human lactalbumin; Molten globule state; NMR; Proline mutagenesis; Protein folding; LA, human lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; DISULFIDE; MUTANT PROTEIN; PROLINE; UREA;

EID: 1842526103     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.02.045     Document Type: Article
Times cited : (17)

References (48)
  • 1
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O.B. Molten globule and protein folding. Advan. Protein Chem. 47:1995;83-229.
    • (1995) Advan. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 2
    • 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
  • 3
    • 0344301982 scopus 로고    scopus 로고
    • Protein folding: A perspective from theory and experiment
    • Dobson C.M., Sali A., Karplus M. Protein folding: a perspective from theory and experiment. Angew. Chem. Int. Ed. 37:1998;868-893.
    • (1998) Angew. Chem. Int. Ed. , vol.37 , pp. 868-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 4
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • Arai M., Kuwajima K. Role of the molten globule state in protein folding. Advan. Protein Chem. 53:2000;209-282.
    • (2000) Advan. Protein Chem. , vol.53 , pp. 209-282
    • Arai, M.1    Kuwajima, K.2
  • 5
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson F.M., Wright P.E., 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
  • 6
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings P.A., 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
  • 7
    • 0030348041 scopus 로고    scopus 로고
    • Rapid formation of a molten globule intermediate in refolding of α-lactalbumin
    • Arai M., Kuwajima K. Rapid formation of a molten globule intermediate in refolding of α-lactalbumin. Fold. Des. 1:1996;275-287.
    • (1996) Fold. Des. , vol.1 , pp. 275-287
    • Arai, M.1    Kuwajima, K.2
  • 9
    • 0342679998 scopus 로고    scopus 로고
    • Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy
    • Trouiller A., Reinstadler D., Dupont Y., Naumann D., Forge V. Transient non-native secondary structures during the refolding of α-lactalbumin detected by infrared spectroscopy. Nature Struct. Biol. 7:2000;78-86.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 78-86
    • Trouiller, A.1    Reinstadler, D.2    Dupont, Y.3    Naumann, D.4    Forge, V.5
  • 10
    • 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
  • 12
    • 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., 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
  • 13
    • 0027280472 scopus 로고
    • Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study
    • Chyan C.L., Wormald C., Dobson C.M., Evans P.A., Baum J. Structure and stability of the molten globule state of guinea-pig α-lactalbumin: a hydrogen exchange study. Biochemistry. 32:1993;5681-5691.
    • (1993) Biochemistry , vol.32 , pp. 5681-5691
    • Chyan, C.L.1    Wormald, C.2    Dobson, C.M.3    Evans, P.A.4    Baum, J.5
  • 14
    • 0028334906 scopus 로고
    • A protein dissection study of a molten globule
    • Peng Z., 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.1    Kim, P.S.2
  • 15
    • 0028916267 scopus 로고
    • Local structural preferences in the α-lactalbumin molten globule
    • Peng Z., Wu L.C., 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.1    Wu, L.C.2    Kim, P.S.3
  • 16
    • 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., Dobson C.M., 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.3    Dobson, C.M.4    Kim, P.S.5
  • 17
    • 0028952169 scopus 로고
    • Bipartite structure of the α-lactalbumin molten globule
    • Wu L.C., Peng Z.-., Kim P.S. Bipartite structure of the α-lactalbumin molten globule. Nature Struct. Biol. 2:1995;281-286.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 281-286
    • Wu, L.C.1    Peng, Z.2    Kim, P.S.3
  • 18
    • 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., Kim P.S. Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology. Nature Struct. Biol. 3:1996;682-687.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 682-687
    • Schulman, B.A.1    Kim, P.S.2
  • 19
    • 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., Redfield C. A residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nature Struct. Biol. 4:1997;630-634.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 20
    • 0031447169 scopus 로고    scopus 로고
    • Hydrophobic sequence minimization of the α-lactalbumin molten globule
    • Wu L.C., Kim P.S. Hydrophobic sequence minimization of the α-lactalbumin molten globule. Proc. Natl Acad. Sci. USA. 94:1997;14314-14319.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 14314-14319
    • Wu, L.C.1    Kim, P.S.2
  • 21
    • 0032479440 scopus 로고    scopus 로고
    • A specific hydrophobic core in the α-lactalbumin molten globule
    • Wu L.C., 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
  • 22
    • 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., Peng Z.-. 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.4
  • 25
    • 0035100811 scopus 로고    scopus 로고
    • A model of dynamic side-chain-side-chain interactions in the α-lactalbumin molten globule
    • Bai P., Song J., Luo L., Peng Z.-. A model of dynamic side-chain-side-chain interactions in the α-lactalbumin molten globule. Protein Sci. 10:2001;55-62.
    • (2001) Protein Sci. , vol.10 , pp. 55-62
    • Bai, P.1    Song, J.2    Luo, L.3    Peng, Z.4
  • 26
    • 0035823118 scopus 로고    scopus 로고
    • Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules
    • Wijesinha-Bettoni R., Dobson C.M., Redfield C. Comparison of the denaturant-induced unfolding of the bovine and human α-lactalbumin molten globules. J. Mol. Biol. 312:2001;261-273.
    • (2001) J. Mol. Biol. , vol.312 , pp. 261-273
    • Wijesinha-Bettoni, R.1    Dobson, C.M.2    Redfield, C.3
  • 27
    • 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., 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
  • 28
    • 0037675760 scopus 로고    scopus 로고
    • Structural characterisation of the human α-lactalbumin molten globule at high temperature
    • Ramboarina S., Redfield C. Structural characterisation of the human α-lactalbumin molten globule at high temperature. J. Mol. Biol. 330:2003;1177-1188.
    • (2003) J. Mol. Biol. , vol.330 , pp. 1177-1188
    • Ramboarina, S.1    Redfield, C.2
  • 29
    • 0026009213 scopus 로고
    • Stable submolecular folding units in a non-compact form of cytochrome c
    • Jeng M.F., Englander S.W. Stable submolecular folding units in a non-compact form of cytochrome c. J. Mol. Biol. 221:1991;1045-1061.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1045-1061
    • Jeng, M.F.1    Englander, S.W.2
  • 30
    • 0028274250 scopus 로고
    • Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronucluear NMR study
    • Alexandrescu A.T., Abeygunawardana C., Shortle D. Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: a heteronucluear NMR study. Biochemistry. 33:1994;1063-1072.
    • (1994) Biochemistry , vol.33 , pp. 1063-1072
    • Alexandrescu, A.T.1    Abeygunawardana, C.2    Shortle, D.3
  • 31
    • 0030726758 scopus 로고    scopus 로고
    • Populating the equilibrium molten globule state of apomyoglobin under suitable conditions for structural characterisation by NMR
    • Eliezar D., Jennings P.A., Dyson H.J., Wright P.E. Populating the equilibrium molten globule state of apomyoglobin under suitable conditions for structural characterisation by NMR. FEBS Letters. 417:1997;92-96.
    • (1997) FEBS Letters , vol.417 , pp. 92-96
    • Eliezar, D.1    Jennings, P.A.2    Dyson, H.J.3    Wright, P.E.4
  • 32
    • 0032539590 scopus 로고    scopus 로고
    • Molten globule unfolding monitored by hydrogen exchange in urea
    • Chamberlain A.K., Marqusee S. Molten globule unfolding monitored by hydrogen exchange in urea. Biochemistry. 37:1998;1736-1742.
    • (1998) Biochemistry , vol.37 , pp. 1736-1742
    • Chamberlain, A.K.1    Marqusee, S.2
  • 33
    • 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., 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
  • 34
    • 0033613115 scopus 로고    scopus 로고
    • The 28-111 disulfide bond constrains the α-lactalbumin molten globule and weakens its cooperativity of folding
    • Luo Y., Baldwin R.L. The 28-111 disulfide bond constrains the α-lactalbumin molten globule and weakens its cooperativity of folding. Proc. Natl Acad. Sci. USA. 96:1999;11283-11287.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11283-11287
    • Luo, Y.1    Baldwin, R.L.2
  • 35
    • 0025182227 scopus 로고
    • Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superactivity of the Cys6-Cys120 disulfide bond
    • Kuwajima K., Ikeguchi M., Sugawara T., Hiraoka Y., Sugai S. Kinetics of disulfide bond reduction in α-lactalbumin by dithiothreitol and molecular basis of superactivity of the Cys6-Cys120 disulfide bond. Biochemistry. 29:1990;8240-8249.
    • (1990) Biochemistry , vol.29 , pp. 8240-8249
    • Kuwajima, K.1    Ikeguchi, M.2    Sugawara, T.3    Hiraoka, Y.4    Sugai, S.5
  • 36
    • 0029894160 scopus 로고    scopus 로고
    • A synthetic peptide study on the molten globule of α-lactalbumin
    • Shimizu A., Ikeguchi M., Kobayashi T., Sugai S. A synthetic peptide study on the molten globule of α-lactalbumin. J. Biochem. 119:1996;947-952.
    • (1996) J. Biochem. , vol.119 , pp. 947-952
    • Shimizu, A.1    Ikeguchi, M.2    Kobayashi, T.3    Sugai, S.4
  • 37
    • 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., 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
  • 38
    • 0032538350 scopus 로고    scopus 로고
    • Peptide models of local and long-range interactions in the molten globule state of human α-lactalbumin
    • Demarest S.J., Fairman R., Raleigh D.P. Peptide models of local and long-range interactions in the molten globule state of human α-lactalbumin. J. Mol. Biol. 283:1998;279-291.
    • (1998) J. Mol. Biol. , vol.283 , pp. 279-291
    • Demarest, S.J.1    Fairman, R.2    Raleigh, D.P.3
  • 39
    • 0034141812 scopus 로고    scopus 로고
    • Solution structure of a peptide model of a region important for the folding of α-lactalbumin provides evidence for the formation of nonnative structure in the denatured state
    • Demarest S.J., Raleigh D.P. Solution structure of a peptide model of a region important for the folding of α-lactalbumin provides evidence for the formation of nonnative structure in the denatured state. Proteins: Struct. Funct. Genet. 38:2000;189-196.
    • (2000) Proteins: Struct. Funct. Genet. , vol.38 , pp. 189-196
    • Demarest, S.J.1    Raleigh, D.P.2
  • 40
    • 0035254984 scopus 로고    scopus 로고
    • A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human α-lactalbumin
    • Demarest S.J., Horng J.-C., Raleigh D.P. A protein dissection study demonstrates that two specific hydrophobic clusters play a key role in stabilizing the core structure of the molten globule state of human α-lactalbumin. Proteins: Struct. Funct. Genet. 42:2001;237-242.
    • (2001) Proteins: Struct. Funct. Genet. , vol.42 , pp. 237-242
    • Demarest, S.J.1    Horng, J.-C.2    Raleigh, D.P.3
  • 41
    • 0033584978 scopus 로고    scopus 로고
    • Defining the core structure of the α-lactalbumin molten globule state
    • Demarest S.J., Boice J.A., Fairman R., Raleigh D.P. Defining the core structure of the α-lactalbumin molten globule state. J. Mol. Biol. 294:1999;213-221.
    • (1999) J. Mol. Biol. , vol.294 , pp. 213-221
    • Demarest, S.J.1    Boice, J.A.2    Fairman, R.3    Raleigh, D.P.4
  • 42
    • 0037132584 scopus 로고    scopus 로고
    • Structural features of the cytochrome c molten globule revealed by fluorescence energy transfer kinetics
    • Lyubovitsky J.G., Gray H.B., Winkler J.R. Structural features of the cytochrome c molten globule revealed by fluorescence energy transfer kinetics. J. Am. Chem. Soc. 124:2002;14840-14841.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14840-14841
    • Lyubovitsky, J.G.1    Gray, H.B.2    Winkler, J.R.3
  • 43
    • 0025891257 scopus 로고
    • Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis
    • Hughson F.M., Barrick D., Baldwin R.L. Probing the stability of a partly folded apomyoglobin intermediate by site-directed mutagenesis. Biochemistry. 30:1991;4113-4118.
    • (1991) Biochemistry , vol.30 , pp. 4113-4118
    • Hughson, F.M.1    Barrick, D.2    Baldwin, R.L.3
  • 44
    • 0033514920 scopus 로고    scopus 로고
    • Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate
    • Kay M.S., Ramos C.H.I., Baldwin R.L. Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate. Proc. Natl Acad. Sci. USA. 96:1999;2007-2012.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2007-2012
    • Kay, M.S.1    Ramos, C.H.I.2    Baldwin, R.L.3
  • 45
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamical characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezar D., Yao J., Dyson H.J., Wright P.E. Structural and dynamical characterization of partially folded states of apomyoglobin and implications for protein folding. Nature Struct. Biol. 5:1998;148-155.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 148-155
    • Eliezar, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 46
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L.E., Keifer P., 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
  • 47
    • 0025210153 scopus 로고
    • Complete resonance assignment for the polypeptide backbone of interleukin 1( using three-dimensional heteronuclear NMR spectroscopy
    • Driscoll P.C., Clore G.M., Marion D., Wingfield P.T., Gronenborn A.M. Complete resonance assignment for the polypeptide backbone of interleukin 1( 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
  • 48
    • 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. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.