메뉴 건너뛰기




Volumn 294, Issue 1, 1999, Pages 213-221

Defining the core structure of the α-lactalbumin molten globule state

Author keywords

Molten globule state; Peptide models; Protein folding; Protein structure; lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; UREA;

EID: 0033584978     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3228     Document Type: Article
Times cited : (55)

References (57)
  • 3
    • 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., 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
  • 4
    • 0027254057 scopus 로고
    • The molten globule intermediate of apomyoglobin and the process of protein folding
    • Barrick D., Baldwin R. L. The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci. 2:1993;869-876.
    • (1993) Protein Sci. , vol.2 , pp. 869-876
    • Barrick, D.1    Baldwin, R.L.2
  • 5
    • 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
  • 7
    • 0025982146 scopus 로고
    • Molten globule intermediates and protein folding
    • Christensen H., Pain H. R. Molten globule intermediates and protein folding. Eur. Biophys. J. 19:1991;221-229.
    • (1991) Eur. Biophys. J. , vol.19 , pp. 221-229
    • Christensen, H.1    Pain, H.R.2
  • 8
    • 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
  • 10
    • 0031026007 scopus 로고    scopus 로고
    • How important is the molten globule for correct protein folding?
    • Creighton T. E. How important is the molten globule for correct protein folding? Trends Biochem. Sci. 22:1997;6-10.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 6-10
    • Creighton, T.E.1
  • 11
    • 0028258026 scopus 로고
    • Disulfide-rearranged molten globule state of α-lactalbumin
    • Creighton T. E., Ewbank J. J. Disulfide-rearranged molten globule state of α-lactalbumin. Biochemistry. 33:1994;1534-1538.
    • (1994) Biochemistry , vol.33 , pp. 1534-1538
    • Creighton, T.E.1    Ewbank, J.J.2
  • 12
    • 0028218304 scopus 로고
    • Folded proteins occur frequently in libraries of random amino acid sequences
    • Davidson A. R., Sauer R. T. Folded proteins occur frequently in libraries of random amino acid sequences. Proc. Natl Acad. Sci. USA. 91:1994;2146-2150.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2146-2150
    • Davidson, A.R.1    Sauer, R.T.2
  • 13
    • 0027190626 scopus 로고
    • An interactive graphic program for calculating the secondary structures/content of proteins from circular dichroism spectrum
    • Deleage G., Geourjon C. An interactive graphic program for calculating the secondary structures/content of proteins from circular dichroism spectrum. CABIOS. 9:1993;197-199.
    • (1993) CABIOS , vol.9 , pp. 197-199
    • Deleage, G.1    Geourjon, C.2
  • 14
    • 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
  • 15
    • 0033153245 scopus 로고    scopus 로고
    • Local interactions drive the formation of non-native structure in the denatured state of human α-lactalbumin: A high resolution structural characterization of a peptide model in aqueous solution
    • Demarest S. J., Hua Y., Raleigh D. P. Local interactions drive the formation of non-native structure in the denatured state of human α-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution. Biochemistry. 38:1999;7380-7387.
    • (1999) Biochemistry , vol.38 , pp. 7380-7387
    • Demarest, S.J.1    Hua, Y.2    Raleigh, D.P.3
  • 18
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer D., Yao J., Dyson H. J., Wright P. E. Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding. Nature Struct. Biology. 5:1998;148-155.
    • (1998) Nature Struct. Biology , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 19
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht A. R. Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7:1997;3-9.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 20
    • 0028174361 scopus 로고
    • Energetics of the α-lactalbumin statets: A calorimetric and statistical thermodynamic study
    • Griko Y. V., Freire E., Privalov P. L. Energetics of the α-lactalbumin statets: a calorimetric and statistical thermodynamic study. Biochemistry. 33:1994;1889-1899.
    • (1994) Biochemistry , vol.33 , pp. 1889-1899
    • Griko, Y.V.1    Freire, E.2    Privalov, P.L.3
  • 21
  • 22
    • 0027053076 scopus 로고
    • Contribution of the 6-120 disulfide bond of α-lactalbumin to the stabilities of the native and molten globule states
    • Ikeguchi M., Sugai S., Fujino M., Sugawara T., Kuwajima K. Contribution of the 6-120 disulfide bond of α-lactalbumin to the stabilities of the native and molten globule states. Biochemistry. 31:1992;12695-12700.
    • (1992) Biochemistry , vol.31 , pp. 12695-12700
    • Ikeguchi, M.1    Sugai, S.2    Fujino, M.3    Sugawara, T.4    Kuwajima, K.5
  • 23
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson S. E. How do small single-domain proteins fold? Fold. Des. 3:1998;R81-R91.
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 24
    • 23444436172 scopus 로고
    • Protein design by binary patterning of polar and nonpolar amino acids
    • Kamtekar S., Schiffer J. M., Xiong H., Babik J. M., Hecht M. H. Protein design by binary patterning of polar and nonpolar amino acids. Science. 262:1993;1680-1685.
    • (1993) Science , vol.262 , pp. 1680-1685
    • Kamtekar, S.1    Schiffer, J.M.2    Xiong, H.3    Babik, J.M.4    Hecht, M.H.5
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A progam to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. MOLSCRIPT: A progam 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.J.1
  • 26
    • 0001305664 scopus 로고
    • Inter- And intramolecular interactions of α-lactalbumin. III. Spectral changes at acid pH
    • Kronman M. J., Cerankowski L., Holmes L. G. Inter- and intramolecular interactions of α-lactalbumin. III. Spectral changes at acid pH. Biochemistry. 4:1965;518-525.
    • (1965) Biochemistry , vol.4 , pp. 518-525
    • Kronman, M.J.1    Cerankowski, L.2    Holmes, L.G.3
  • 27
    • 0014209816 scopus 로고
    • Inter- And intramolecular interactions of α-lactalbumin. VIII. The alkaline conformational change
    • Kronman M. J., Holmes L. G., Robbins F. M. Inter- and intramolecular interactions of α-lactalbumin. VIII. The alkaline conformational change. Biochim. Biophys. Acta. 133:1967;46-55.
    • (1967) Biochim. Biophys. Acta , vol.133 , pp. 46-55
    • Kronman, M.J.1    Holmes, L.G.2    Robbins, F.M.3
  • 28
    • 0030993346 scopus 로고    scopus 로고
    • Calcium binding peptides from α- lactalbumin: Implications for protein folding
    • Kuhlman B., Wu W.-J., Boice J., Fairman R., Raleigh D. P. Calcium binding peptides from α- lactalbumin: implications for protein folding. Biochemistry. 36:1997;4607-4615.
    • (1997) Biochemistry , vol.36 , pp. 4607-4615
    • Kuhlman, B.1    Wu, W.-J.2    Boice, J.3    Fairman, R.4    Raleigh, D.P.5
  • 29
    • 0032570265 scopus 로고    scopus 로고
    • Structure and stability of the N-terminal domain of the ribosomal protein L9: Evidence for rapid two-state folding
    • Kuhlman B., Boice J., Fairman R., Raleigh D. P. Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding. Biochemistry. 37:1998;1025-1032.
    • (1998) Biochemistry , vol.37 , pp. 1025-1032
    • Kuhlman, B.1    Boice, J.2    Fairman, R.3    Raleigh, D.P.4
  • 30
    • 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;102-108.
    • (1996) FASEB J. , vol.10 , pp. 102-108
    • Kuwajima, K.1
  • 31
    • 0016812050 scopus 로고
    • Electrophoretic investigations of the acid conformational change of α-lactalbumin
    • Kuwajima K., Nitta K., Sugai S. Electrophoretic investigations of the acid conformational change of α-lactalbumin. J. Biochem. 78:1975;205-211.
    • (1975) J. Biochem. , vol.78 , pp. 205-211
    • Kuwajima, K.1    Nitta, K.2    Sugai, S.3
  • 32
    • 0017178548 scopus 로고
    • Three state denaturation of α-lactalbumin by guanidine hydrochloride
    • Kuwajima K., Nitta K., Yoneyama M., Sugai S. Three state denaturation of α-lactalbumin by guanidine hydrochloride. J. Mol. Biol. 106:1976;359-373.
    • (1976) J. Mol. Biol. , vol.106 , pp. 359-373
    • Kuwajima, K.1    Nitta, K.2    Yoneyama, M.3    Sugai, S.4
  • 33
    • 0024596024 scopus 로고
    • 2+ binding on the folding kinetics of α-lactalbumin
    • 2+ binding on the folding kinetics of α-lactalbumin. J. Mol. Biol. 206:1989;547-561.
    • (1989) J. Mol. Biol. , vol.206 , pp. 547-561
    • Kuwajima, K.1    Mitani, M.2    Sugai, S.3
  • 34
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers J. K., Pace C. N., Scholtz J. M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 35
    • 0023692599 scopus 로고
    • A peptide model of a protein folding intermediate
    • Oas T. G., Kim P. S. A peptide model of a protein folding intermediate. Nature. 336:1988;42-48.
    • (1988) Nature , vol.336 , pp. 42-48
    • Oas, T.G.1    Kim, P.S.2
  • 36
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace C. N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 37
    • 0028871804 scopus 로고
    • How to measure the molar absorption coefficient of a protein
    • Pace C. N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure the molar absorption coefficient of a protein. Protein Sci. 4:1995;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
  • 38
    • 0028334906 scopus 로고
    • A protein dissection study of a molten globule
    • Peng Z.-y., 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
  • 39
    • 0028916267 scopus 로고
    • Local structural preferences in the α-lactalbumin molten globule
    • Peng Z.-y., 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.-y.1    Wu, L.C.2    Kim, P.S.3
  • 40
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • Ptitsyn O. B. Molten globule and protein folding. Advan. Protein Chem. 47:1995;83-217.
    • (1995) Advan. Protein Chem. , vol.47 , pp. 83-217
    • Ptitsyn, O.B.1
  • 41
    • 0029157648 scopus 로고
    • A de novo designed protein mimics the native state of natural proteins
    • Raleigh D. P., Betz S. F., Degrado W. F. A de novo designed protein mimics the native state of natural proteins. J. Am. Chem. Soc. 117:1995;7558-7559.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 7558-7559
    • Raleigh, D.P.1    Betz, S.F.2    Degrado, W.F.3
  • 42
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • Raschke T. M., Marqusee S. The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Struct. Biol. 4:1997;298-304.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 43
    • 0030874298 scopus 로고    scopus 로고
    • Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of helix-coil transition in peptides
    • Rohl C. A., Baldwin R. L. Comparison of NH exchange and circular dichroism as techniques for measuring the parameters of helix-coil transition in peptides. Biochemistry. 36:1997;8435-8442.
    • (1997) Biochemistry , vol.36 , pp. 8435-8442
    • Rohl, C.A.1    Baldwin, R.L.2
  • 44
    • 0029765444 scopus 로고    scopus 로고
    • Proline scanning mutagenesis study of a molten globule reveals non-cooperative formation of a protein's overall topology
    • Schulman B. A., Kim P. S. Proline scanning mutagenesis study 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
  • 45
    • 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
  • 48
    • 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
  • 49
    • 0028774041 scopus 로고
    • Solution structure of a peptide fragment of human α-lactalbumin in trifluoroethanol: A model for local structure in the molten globule
    • Smith L. J., Alexandrescu A. T., Pitkeathly M., Dobson C. M. Solution structure of a peptide fragment of human α-lactalbumin in trifluoroethanol: a model for local structure in the molten globule. Structure. 2:1995;703-712.
    • (1995) Structure , vol.2 , pp. 703-712
    • Smith, L.J.1    Alexandrescu, A.T.2    Pitkeathly, M.3    Dobson, C.M.4
  • 50
    • 0019000261 scopus 로고
    • Comparative fluorescence properties of bovine, goat, human and guinea pig α-lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers
    • Sommers P. B., Kronman M. J. Comparative fluorescence properties of bovine, goat, human and guinea pig α-lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers. Biophys. Chem. 11:1980;217-232.
    • (1980) Biophys. Chem. , vol.11 , pp. 217-232
    • Sommers, P.B.1    Kronman, M.J.2
  • 51
    • 0032479326 scopus 로고    scopus 로고
    • Contribution of individual residues to formation of the native-like topology in the α-lactalbumin molten globule
    • Song J., Bai P., Luo L., Peng Z.-y. Contribution of individual residues to formation of the native-like 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
  • 52
    • 0025271083 scopus 로고
    • Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor
    • Staley J. P., Kim P. S. Role of a subdomain in the folding of bovine pancreatic trypsin inhibitor. Nature. 344:1990;685-688.
    • (1990) Nature , vol.344 , pp. 685-688
    • Staley, J.P.1    Kim, P.S.2
  • 53
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford C. Protein denaturation. C. Theoretical models for the mechanism of denaturation. Advan. Protein Chem. 24:1970;1-95.
    • (1970) Advan. Protein Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 54
    • 0029612267 scopus 로고
    • Effects of amino acid substitutions in the hydrophobic core of α-lactalbumin to the stabilities of the molten globule state
    • Uchiyama H., Perez-Prat E. M., Watanabe K., Kumagai I., Kuwajima K. Effects of amino acid substitutions in the hydrophobic core of α-lactalbumin to the stabilities of the molten globule state. Protein Eng. 8:1995;1153-1161.
    • (1995) Protein Eng. , vol.8 , pp. 1153-1161
    • Uchiyama, H.1    Perez-Prat, E.M.2    Watanabe, K.3    Kumagai, I.4    Kuwajima, K.5
  • 55
    • 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
  • 56
    • 0027442944 scopus 로고
    • A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c
    • Wu L. C., Laub P. B., Elove G. A., Carey J., Roder H. A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry. 32:1993;10271-10276.
    • (1993) Biochemistry , vol.32 , pp. 10271-10276
    • Wu, L.C.1    Laub, P.B.2    Elove, G.A.3    Carey, J.4    Roder, H.5
  • 57
    • 0028952169 scopus 로고
    • Bipartite structure of the α-lactalbumin molten globule
    • Wu L. C., Peng Z.-y., Kim P. S. Bipartite structure of the α-lactalbumin molten globule. Nature Struct. Biol. 2:1995;281-285.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 281-285
    • Wu, L.C.1    Peng, Z.-y.2    Kim, P.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.