메뉴 건너뛰기




Volumn 286, Issue 5, 1999, Pages 1567-1580

Side-chain conformational disorder in a molten globule: Molecular dynamics simulations of the A-state of human α-lactalbumin

Author keywords

Computer simulation; Molecular dynamics; Molten globule; Protein folding; lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; CALCIUM;

EID: 0033548540     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2545     Document Type: Article
Times cited : (37)

References (41)
  • 3
    • 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. Design. 1:1996;275-287.
    • (1996) Fold. Design , vol.1 , pp. 275-287
    • Arai, M.1    Kuwajima, K.2
  • 5
    • 0024533979 scopus 로고
    • Characterisation 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. Characterisation 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
  • 8
    • 0027249641 scopus 로고
    • De novo protein design - From molten globules to native-like states
    • Betz S. F., Raleigh D. P., Degrado W. F. De novo protein design - from molten globules to native-like states. Curr. Opin. Struct. Biol. 3:1993;601-610.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 601-610
    • Betz, S.F.1    Raleigh, D.P.2    Degrado, W.F.3
  • 9
    • 0027411263 scopus 로고
    • Molecular simulations of peptide and protein unfolding - In quest of a molten globule
    • Brooks C. L. Molecular simulations of peptide and protein unfolding - in quest of a molten globule. Curr. Opin. Struct. Biol. 3:1993;92-98.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 92-98
    • Brooks, C.L.1
  • 11
    • 0028466243 scopus 로고
    • Protein folding - Solid evidence for molten globules
    • Dobson C. M. Protein folding - solid evidence for molten globules. Curr. Biol. 4:1994;636-640.
    • (1994) Curr. Biol. , vol.4 , pp. 636-640
    • Dobson, C.M.1
  • 12
    • 0029117494 scopus 로고
    • Finding the right fold
    • Dobson C. M. Finding the right fold. Nature Struct. Biol. 2:1995;513-517.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 513-517
    • Dobson, C.M.1
  • 13
    • 0344382167 scopus 로고
    • Characterisation of unfolded and partially folded states of proteins by NMR spectroscopy
    • B. T. Nall, & K. A. Dill. Washington DC: AAAS Publications
    • Dobson C. M., Hanley C., Radford S. E., Baum J., Evans P. A. Characterisation of unfolded and partially folded states of proteins by NMR spectroscopy. Nall B. T., Dill K. A. Conformations and Forces in Protein Folding. 1991;175-181 AAAS Publications, Washington DC.
    • (1991) Conformations and Forces in Protein Folding , pp. 175-181
    • Dobson, C.M.1    Hanley, C.2    Radford, S.E.3    Baum, J.4    Evans, P.A.5
  • 14
    • 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. Edit. 37:1998;868-893.
    • (1998) Angew. Chem. Int. Edit. , vol.37 , pp. 868-893
    • Dobson, C.M.1    Sali, A.2    Karplus, M.3
  • 17
    • 0028429178 scopus 로고
    • Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains
    • Dunbrack R. L., Karplus M. Conformational analysis of the backbone-dependent rotamer preferences of protein sidechains. Nature Struct. Biol. 1:1994;334-340.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 334-340
    • Dunbrack, R.L.1    Karplus, M.2
  • 18
    • 0001529088 scopus 로고
    • Quasielastic light scattering from human α-lactalbumin: Comparison of molecular dimensions in native and molten globule states
    • Gast K., Zirwer D., Welfle H., Bychkova V. E., Ptitsyn O. B. Quasielastic light scattering from human α-lactalbumin: comparison of molecular dimensions in native and molten globule states. Int. J. Biol. Macromol. 8:1986;231-236.
    • (1986) Int. J. Biol. Macromol. , vol.8 , pp. 231-236
    • Gast, K.1    Zirwer, D.2    Welfle, H.3    Bychkova, V.E.4    Ptitsyn, O.B.5
  • 19
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • Gillespie J. R., Shortle D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. J. Mol. Biol. 268:1997;170-184.
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 20
    • 0003742069 scopus 로고
    • London: Departments of Biochemistry and Molecular BiologyUniversity College
    • Hubbard S. J., Thornton J. M. NACCESS Computer Program. 1993;Departments of Biochemistry and Molecular BiologyUniversity College, London.
    • (1993) NACCESS Computer Program
    • Hubbard, S.J.1    Thornton, J.M.2
  • 21
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen bonded and geometrical features
    • Kabsch W., Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen bonded and geometrical features. Biopolymers. 22:1983;2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 22
    • 0031019791 scopus 로고    scopus 로고
    • Molten globule of human α-lactalbumin: Hydration, density and compressibility of the interior
    • Kharakoz D. P., Bychkova V. E. Molten globule of human α-lactalbumin: hydration, density and compressibility of the interior. Biochemistry. 36:1997;1882-1890.
    • (1997) Biochemistry , vol.36 , pp. 1882-1890
    • Kharakoz, D.P.1    Bychkova, V.E.2
  • 23
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. J. 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.J.1
  • 24
    • 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: Struct. Funct. Genet. 6:1989;87-103.
    • (1989) Proteins: Struct. Funct. Genet , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 25
    • 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
  • 26
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
    • Kuwajima K., Hiraoka Y., Ikeguchi M., Sugai S. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry. 24:1985;874-881.
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 27
    • 0021691918 scopus 로고
    • An analysis of incorrectly folded protein models. Implications for structure prediction
    • Novotny J., Bruccoleri R., Karplus M. An analysis of incorrectly folded protein models. Implications for structure prediction. J. Mol. Biol. 177:1984;787-818.
    • (1984) J. Mol. Biol. , vol.177 , pp. 787-818
    • Novotny, J.1    Bruccoleri, R.2    Karplus, M.3
  • 28
    • 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
  • 29
    • 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
  • 30
    • 33646940952 scopus 로고
    • Numerical intergration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • Ryckaert J. P., Ciccotti G., Berendsen H. J. C. Numerical intergration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes. J. Comput. Phys. 23:1977;327-341.
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 31
    • 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., 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
  • 32
    • 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
  • 33
    • 0030320442 scopus 로고    scopus 로고
    • The concept of a random coil. Residual structure in peptides and denatured proteins
    • Smith L. J., Fiebig K. M., Schwalbe H., Dobson C. M. The concept of a random coil. Residual structure in peptides and denatured proteins. Fold. Design. 1:1996;R95-R106.
    • (1996) Fold. Design , vol.1
    • Smith, L.J.1    Fiebig, K.M.2    Schwalbe, H.3    Dobson, C.M.4
  • 34
    • 0029147823 scopus 로고
    • Intrinsic φ, ψ propensities of amino acids derived from the coil region of known structures
    • Swindells M. B., MacArthur M. W., Thornton J. M. Intrinsic φ, ψ propensities of amino acids derived from the coil region of known structures. Nature Struct. Biol. 2:1995;596-603.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 596-603
    • Swindells, M.B.1    MacArthur, M.W.2    Thornton, J.M.3
  • 36
    • 2142813682 scopus 로고
    • Computer simulation of molecular dynamics - Methodology, applications, and perspectives in chemistry
    • van Gunsteren W. F., Berendsen H. J. C. Computer simulation of molecular dynamics - methodology, applications, and perspectives in chemistry. Angew. Chem. Int. Edit. 29:1990;992-1023.
    • (1990) Angew. Chem. Int. Edit. , vol.29 , pp. 992-1023
    • Van Gunsteren, W.F.1    Berendsen, H.J.C.2
  • 39
    • 44949269218 scopus 로고
    • Empirical comparisons of models for chemical-shift calculation in proteins
    • Williamson M. P., Asakura T. Empirical comparisons of models for chemical-shift calculation in proteins. J. Magn. Reson. ser. B. 101:1993;63-71.
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 63-71
    • Williamson, M.P.1    Asakura, T.2
  • 40
    • 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
  • 41
    • 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;281-286.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 281-286
    • Wu, L.C.1    Peng, Z.Y.2    Kim, P.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.