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Volumn 350, Issue 4, 2005, Pages 817-829

Probing the "annealing" mechanism of GroEL minichaperone using molecular dynamics simulations

Author keywords

GroEL minichaperone; MD simulations; Protein protein interactions; Transient binding release mechanism

Indexed keywords

CASEIN; CHAPERONE; PROTEIN; PROTEIN GROEL; UNCLASSIFIED DRUG;

EID: 20544466881     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.05.012     Document Type: Article
Times cited : (26)

References (30)
  • 2
    • 0027144068 scopus 로고
    • Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP
    • Y. Makino, H. Taguchi, and M. Yoshida Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP FEBS Letters 336 1993 363 367
    • (1993) FEBS Letters , vol.336 , pp. 363-367
    • Makino, Y.1    Taguchi, H.2    Yoshida, M.3
  • 4
    • 0032514615 scopus 로고    scopus 로고
    • GroEL-GroES-mediated protein folding requires an intact central cavity
    • J.D. Wang, M.D. Michelitsch, and J.S. Weissman GroEL-GroES-mediated protein folding requires an intact central cavity Proc. Natl Acad. Sci. USA 95 1998 12163 12168
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12163-12168
    • Wang, J.D.1    Michelitsch, M.D.2    Weissman, J.S.3
  • 5
    • 0030006212 scopus 로고    scopus 로고
    • Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
    • M.J. Todd, G.H. Lorimer, and D. Thirumalai Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism Proc. Natl Acad. Sci. USA 93 1996 4030 4035
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4030-4035
    • Todd, M.J.1    Lorimer, G.H.2    Thirumalai, D.3
  • 7
    • 0033515436 scopus 로고    scopus 로고
    • Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity
    • M.R. Betancourt, and D. Thirumalai Exploring the kinetic requirements for enhancement of protein folding rates in the GroEL cavity J. Mol. Biol. 287 1999 627 644
    • (1999) J. Mol. Biol. , vol.287 , pp. 627-644
    • Betancourt, M.R.1    Thirumalai, D.2
  • 9
    • 11144240550 scopus 로고    scopus 로고
    • A kinetic model for chaperonin assisted protein folding
    • H. Orland, and D. Thirumalai A kinetic model for chaperonin assisted protein folding J. Phys. 7 1997 533 560
    • (1997) J. Phys. , vol.7 , pp. 533-560
    • Orland, H.1    Thirumalai, D.2
  • 10
    • 4444330162 scopus 로고    scopus 로고
    • Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: Creation of an alternate fast folding pathway
    • A.I. Jewett, A. Baumketner, and J.E. Shea Accelerated folding in the weak hydrophobic environment of a chaperonin cavity: creation of an alternate fast folding pathway Proc. Natl Acad. Sci. USA 101 2004 13192 13197
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 13192-13197
    • Jewett, A.I.1    Baumketner, A.2    Shea, J.E.3
  • 11
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
    • L. Chen, and P.B. Sigler The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity Cell 99 1999 757 768
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 13
    • 0037438479 scopus 로고    scopus 로고
    • Annealing function of GroEL: Structural and bioinformatic analysis
    • G. Stan, D. Thirumalai, G.H. Lorimer, and B.R. Brooks Annealing function of GroEL: structural and bioinformatic analysis Biophys. Chem. 100 2003 453 467
    • (2003) Biophys. Chem. , vol.100 , pp. 453-467
    • Stan, G.1    Thirumalai, D.2    Lorimer, G.H.3    Brooks, B.R.4
  • 14
    • 0026119905 scopus 로고
    • Ergodic measures for the simulation for dielectric properties of water
    • R.D. Mountain, and D. Thirumalai Ergodic measures for the simulation for dielectric properties of water Comput. Phys. Commun. 62 1991 352 359
    • (1991) Comput. Phys. Commun. , vol.62 , pp. 352-359
    • Mountain, R.D.1    Thirumalai, D.2
  • 15
    • 0030966765 scopus 로고    scopus 로고
    • A structural model for GroEL-polypeptide recognition
    • A.M. Buckle, R. Zahn, and A.R. Fersht A structural model for GroEL-polypeptide recognition Proc. Natl Acad. Sci. USA 94 1997 3571 3575
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3571-3575
    • Buckle, A.M.1    Zahn, R.2    Fersht, A.R.3
  • 16
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • M. Shtilerman, G.H. Lorimer, and S.W. Englander Chaperonin function: folding by forced unfolding Science 284 1999 822 825
    • (1999) Science , vol.284 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 17
    • 3042856284 scopus 로고    scopus 로고
    • The unfolding action of GroEL on a protein substrate
    • A. van der Vaart, J. Ma, and M. Karplus The unfolding action of GroEL on a protein substrate Biophys. J. 87 2004 562 573
    • (2004) Biophys. J. , vol.87 , pp. 562-573
    • Van Der Vaart, A.1    Ma, J.2    Karplus, M.3
  • 18
    • 0035913910 scopus 로고    scopus 로고
    • GroEL/GroES-mediated folding of a protein too large to be encapsulated
    • T.K. Chaudhuri, G.W. Farr, W.A. Fenton, S. Rospert, and A.L. Horwich GroEL/GroES-mediated folding of a protein too large to be encapsulated Cell 107 2001 223 233
    • (2001) Cell , vol.107 , pp. 223-233
    • Chaudhuri, T.K.1    Farr, G.W.2    Fenton, W.A.3    Rospert, S.4    Horwich, A.L.5
  • 19
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte, and R.F. Doolittle A simple method for displaying the hydropathic character of a protein J. Mol. Biol. 157 1982 105 132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 20
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • D. Eisenberg, E. Schwartz, M. Komaromy, and R. Wall Analysis of membrane and surface protein sequences with the hydrophobic moment plot J. Mol. Biol. 179 1984 125 142
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisenberg, D.1    Schwartz, E.2    Komaromy, M.3    Wall, R.4
  • 21
    • 0032964297 scopus 로고    scopus 로고
    • BLAST 2 sequences, a new tool for comparing protein and nucleotide sequences
    • T.A. Tatusova, and T.L. Madden BLAST 2 sequences, a new tool for comparing protein and nucleotide sequences FEMS Microbiol. Letters 174 1999 247 250
    • (1999) FEMS Microbiol. Letters , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 23
    • 0027291015 scopus 로고
    • Prediction of protein structure at better than 70% accuracy
    • B. Rost, and C. Sander Prediction of protein structure at better than 70% accuracy J. Mol. Biol. 232 1993 584 599
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 25
    • 0041784950 scopus 로고    scopus 로고
    • All-hydrogen empirical potential for molecular modeling and dynamics studies of proteins using the CHARMM22 force field
    • A.D. MacKerell Jr, D. Bashford, M. Bellott, R.L. Dunbrack Jr, J. Evanseck, and M.J. Field All-hydrogen empirical potential for molecular modeling and dynamics studies of proteins using the CHARMM22 force field J. Phys. Chem. B 102 1998 3586 3616
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell Jr., A.D.1    Bashford, D.2    Bellott, M.3    Dunbrack Jr., R.L.4    Evanseck, J.5    Field, M.J.6
  • 29
    • 36849111485 scopus 로고
    • Shape of a self-avoiding walk or polymer chain
    • M.E. Fisher Shape of a self-avoiding walk or polymer chain J. Chem. Phys. 44 1966 616 622
    • (1966) J. Chem. Phys. , vol.44 , pp. 616-622
    • Fisher, M.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.