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Volumn 405, Issue 6782, 2000, Pages 39-42

A surprising simplicity to protein folding

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; MOLECULAR DYNAMICS; MOLECULAR MODEL; PHYSICS; PREDICTION; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN STRUCTURE;

EID: 0034604105     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/35011000     Document Type: Article
Times cited : (672)

References (44)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinson, C. Principles that govern the folding of protein chains. Science 181, 223-227 (1973).
    • (1973) Science , vol.181 , pp. 223-227
    • Anfinson, C.1
  • 2
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • Baldwin, R. L. & Rose, G. D. Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 24, 26-33 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2
  • 3
    • 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, R81-91 (1998).
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 5
    • 0003166498 scopus 로고    scopus 로고
    • Protein folding in the landscape perspective: Chevron plots and non-Arrhenius kinetics
    • Chan, H. S. & Dill, K. A. Protein folding in the landscape perspective: chevron plots and non-Arrhenius kinetics. Proteins 30, 2-33 (1998).
    • (1998) Proteins , vol.30 , pp. 2-33
    • Chan, H.S.1    Dill, K.A.2
  • 6
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson, J. D., Onuchic, J. N., Socci, N. D. & Wolynes, P. G. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 21, 167-195 (1995).
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 7
    • 0032842870 scopus 로고    scopus 로고
    • The fundamentals of protein folding: Bringing together theory and experiment
    • Dobson, C. M. & Karplus, M. The fundamentals of protein folding: bringing together theory and experiment. Curr. Opin. Struct. Biol. 9, 92-101 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 92-101
    • Dobson, C.M.1    Karplus, M.2
  • 8
    • 0033613184 scopus 로고    scopus 로고
    • Chaperone rings in protein folding and degradation
    • Horwich, A. L. Chaperone rings in protein folding and degradation. Proc. Natl Acad. Sci. USA 96, 11033-11040 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11033-11040
    • Horwich, A.L.1
  • 9
    • 0032444334 scopus 로고    scopus 로고
    • Folding nucleus: Specific or multiple? Insights from lattice models and experiments
    • Shakhnovich, E. I. Folding nucleus: specific or multiple? Insights from lattice models and experiments. Fold. Des. 3, R108-111 (1998).
    • (1998) Fold. Des. , vol.3
    • Shakhnovich, E.I.1
  • 11
    • 0032428359 scopus 로고    scopus 로고
    • Fishing for folding nuclei in lattice models and proteins
    • Thirumalai, D. & Klimov, D. K. Fishing for folding nuclei in lattice models and proteins. Fold. Des. 3, R112-118 (1998).
    • (1998) Fold. Des. , vol.3
    • Thirumalai, D.1    Klimov, D.K.2
  • 12
    • 0033117763 scopus 로고    scopus 로고
    • Matching theory and experiment in protein folding
    • Alm, E. & Baker, D. Matching theory and experiment in protein folding. Curr. Opin. Struct. Biol. 9, 189-196 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 189-196
    • Alm, E.1    Baker, D.2
  • 13
    • 0030852463 scopus 로고    scopus 로고
    • Functional rapidly folding proteins from simplified amino acid sequences
    • Riddle, D. S. et al. Functional rapidly folding proteins from simplified amino acid sequences. Nature Struct. Biol. 4, 805-809 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 805-809
    • Riddle, D.S.1
  • 14
    • 0032574811 scopus 로고    scopus 로고
    • The sequences of small proteins are not extensively optimized for rapid folding by natural selection
    • Kim, D. E., Gu, H. & Baker, D. The sequences of small proteins are not extensively optimized for rapid folding by natural selection. Prac. Natl Acad. Sci. USA 95, 4982-4986 (1998).
    • (1998) Prac. Natl Acad. Sci. USA , vol.95 , pp. 4982-4986
    • Kim, D.E.1    Gu, H.2    Baker, D.3
  • 15
    • 0031890195 scopus 로고    scopus 로고
    • Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins
    • Perl, D. et al. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nature Struct. Biol. 5, 229-235 (1998).
    • (1998) Nature Struct. Biol. , vol.5 , pp. 229-235
    • Perl, D.1
  • 16
    • 0032708771 scopus 로고    scopus 로고
    • Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding
    • Chiti, F. et al. Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding. Nature Struct. Biol. 6, 1005-1009 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1005-1009
    • Chiti, F.1
  • 17
    • 0032750509 scopus 로고    scopus 로고
    • The folding transition state between SH3 domains is conformationally restricted and evolutionary conserved
    • Martinez, J. C. & Serrano, L. The folding transition state between SH3 domains is conformationally restricted and evolutionary conserved. Nature Struct. Biol. 6, 1010-1016 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1010-1016
    • Martinez, J.C.1    Serrano, L.2
  • 18
    • 0032734515 scopus 로고    scopus 로고
    • Experiment and theory highlight role of native state topology in SH3 folding
    • Riddle, D. S. et al. Experiment and theory highlight role of native state topology in SH3 folding. Nature Struct. Biol. 6, 1016-1024 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 1016-1024
    • Riddle, D.S.1
  • 19
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., Simons, K. T. & Baker, D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277, 985-994 (1998).
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 20
    • 0033607208 scopus 로고    scopus 로고
    • Exploring the origins of topological frustration: Design of a minimally frustrated model of fragment B of protein A
    • Shea J. E., Onuchic J. N. & Brooks, C. L. III. Exploring the origins of topological frustration: design of a minimally frustrated model of fragment B of protein A. Proc. Natl Acad. Sci. USA 96, 12512-12517 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 12512-12517
    • Shea, J.E.1    Onuchic, J.N.2    Brooks C.L. III3
  • 21
    • 0034581317 scopus 로고    scopus 로고
    • The energy landscape theory of protein folding: Insights into folding mechanism and scenarios
    • Onuch, J. N., Nymeyer, H., Garcia, A. E., Chaine, J. & Socci, N. D. The energy landscape theory of protein folding: insights into folding mechanism and scenarios. Adv. Protein Chem. 53, 87-152 (2000).
    • (2000) Adv. Protein Chem. , vol.53 , pp. 87-152
    • Onuch, J.N.1    Nymeyer, H.2    Garcia, A.E.3    Chaine, J.4    Socci, N.D.5
  • 22
    • 18344391877 scopus 로고    scopus 로고
    • Protein structures and optimal folding from a geometrical variational principle
    • Micheletti, C., Banavar, J. R., Maritan, A. & Seno, F. Protein structures and optimal folding from a geometrical variational principle. Phys. Rev. Lett. 82, 3372-3375 (1999).
    • (1999) Phys. Rev. Lett. , vol.82 , pp. 3372-3375
    • Micheletti, C.1    Banavar, J.R.2    Maritan, A.3    Seno, F.4
  • 23
    • 0028024928 scopus 로고
    • Specific nucleus as the transition state for protein folding: Evidence from the lattice model
    • Abkevich, V., Gutin, A. & Shakhnovich, E. Specific nucleus as the transition state for protein folding: evidence from the lattice model. Biochemistry 33, 10026-10036 (1994).
    • (1994) Biochemistry , vol.33 , pp. 10026-10036
    • Abkevich, V.1    Gutin, A.2    Shakhnovich, E.3
  • 24
    • 0033613165 scopus 로고    scopus 로고
    • A simple model for calculating the kinetics of protein folding from three-dimensional structures
    • Munoz, V. & Eaton, W. A. A simple model for calculating the kinetics of protein folding from three-dimensional structures. Proc. Natl Acad. Sci. USA 96, 11311-11316 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11311-11316
    • Munoz, V.1    Eaton, W.A.2
  • 25
    • 0033613131 scopus 로고    scopus 로고
    • A theoretical search for folding/unfolding nuclei in three-dimensional protein structures
    • Galzitskaya, O. V. & Finkelstein, A. V. A theoretical search for folding/unfolding nuclei in three-dimensional protein structures. Proc. Natl Acad. Sci. USA 96, 11299-11304 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11299-11304
    • Galzitskaya, O.V.1    Finkelstein, A.V.2
  • 26
    • 0033613255 scopus 로고    scopus 로고
    • Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures
    • Alm, E. & Baker, D. Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures. Proc. Natl Acad. Sci. USA 96, 11305-11310(1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11305-11310
    • Alm, E.1    Baker, D.2
  • 27
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • Go, N. Theoretical studies of protein folding. Annu. Rev. Biophys. Bioeng. 12, 183-210 (1983).
    • (1983) Annu. Rev. Biophys. Bioeng. , vol.12 , pp. 183-210
    • Go, N.1
  • 28
    • 0000227308 scopus 로고    scopus 로고
    • Variational theory for site resolved protein folding free energy surfaces
    • Portman J. J., Takada, S. & Wolynes, P. G Variational theory for site resolved protein folding free energy surfaces. Phys. Rev. Lett. 81, 5237-5240 (1998).
    • (1998) Phys. Rev. Lett. , vol.81 , pp. 5237-5240
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 29
    • 0033521194 scopus 로고    scopus 로고
    • First principles prediction of protein-folding rates
    • Debye, D & Goddard, W. A. First principles prediction of protein-folding rates. J. Mol. Biol. 294, 619-625 (1999).
    • (1999) J. Mol. Biol. , vol.294 , pp. 619-625
    • Debye, D.1    Goddard, W.A.2
  • 30
    • 0029963345 scopus 로고    scopus 로고
    • Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations
    • Li, A. J. & Daggett, V. Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations. J. Mol. Biol. 257, 412-429 (1996).
    • (1996) J. Mol. Biol. , vol.257 , pp. 412-429
    • Li, A.J.1    Daggett, V.2
  • 31
    • 0031465967 scopus 로고    scopus 로고
    • 'New view' ot protein folding reconciled with the old through multiple unfolding simulations
    • Lazaridis, T. & Karplus, M. 'New view' ot protein folding reconciled with the old through multiple unfolding simulations. Science 278, 1928-1931 (1997).
    • (1997) Science , vol.278 , pp. 1928-1931
    • Lazaridis, T.1    Karplus, M.2
  • 32
    • 0030982583 scopus 로고    scopus 로고
    • A molecular dynamics simulation study of segment B1 of protein G
    • Sheinerman, F. B. & Brooks, C. L. III A molecular dynamics simulation study of segment B1 of protein G. Proteins 29, 193-202 (1997).
    • (1997) Proteins , vol.29 , pp. 193-202
    • Sheinerman, F.B.1    Brooks C.L. III2
  • 33
    • 0032554626 scopus 로고    scopus 로고
    • Protein folding dynamics: Quantitative comparison between theory and experiment
    • Burton, R. E., Myers, J. K. & Oas, T. G. Protein folding dynamics: quantitative comparison between theory and experiment. Biochemistry 37, 5337-5343 (1998).
    • (1998) Biochemistry , vol.37 , pp. 5337-5343
    • Burton, R.E.1    Myers, J.K.2    Oas, T.G.3
  • 34
    • 0032606039 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction (CASP): Round III
    • Moult, J., Hubbard, T., Fidelis, K. & Pederson, J. T. Critical assessment of methods of protein structure prediction (CASP): round III. Proteins (Suppl.) 3, 2-6 (1999).
    • (1999) Proteins (Suppl.) , vol.3 , pp. 2-6
    • Moult, J.1    Hubbard, T.2    Fidelis, K.3    Pederson, J.T.4
  • 35
    • 0032828469 scopus 로고    scopus 로고
    • Analysis and assessmeni of ab initio three-dimensional prediction, secondary structure, and contacts prediction
    • Orengo, C. A., Bray, J. E., Hubbard, T. LoConte, L. & Sillitoe, I. Analysis and assessmeni of ab initio three-dimensional prediction, secondary structure, and contacts prediction. Proteins (Suppl.) 3, 149-170 (1999).
    • (1999) Proteins (Suppl.) , vol.3 , pp. 149-170
    • Orengo, C.A.1    Bray, J.E.2    Hubbard, T.3    LoConte, L.4    Sillitoe, I.5
  • 36
    • 0032605908 scopus 로고    scopus 로고
    • Structure classification-based assessment of CASP3 predictions for the fold recognition targets
    • Murzin, A. G. Structure classification-based assessment of CASP3 predictions for the fold recognition targets. Proteins (Suppl.) 3, 88-103 (1999).
    • (1999) Proteins (Suppl.) , vol.3 , pp. 88-103
    • Murzin, A.G.1
  • 37
    • 0032515105 scopus 로고    scopus 로고
    • Structure of the transition state in the folding process of human procarboxypeptidase A2 retivation domain
    • Villegas, V., Martinez, J. C., Aviles, F. X. & Serrano, L. Structure of the transition state in the folding process of human procarboxypeptidase A2 retivation domain. J. Mol. Biol. 283, 1027-1036 (1998).
    • (1998) J. Mol. Biol. , vol.283 , pp. 1027-1036
    • Villegas, V.1    Martinez, J.C.2    Aviles, F.X.3    Serrano, L.4
  • 38
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, Cl-2
    • Lopez-Hernandez, E. & Serrano, L. Structure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller protein, Cl-2. Fold. Des. 1, 43-55 (1996).
    • (1996) Fold. Des. , vol.1 , pp. 43-55
    • Lopez-Hernandez, E.1    Serrano, L.2
  • 39
    • 0032612579 scopus 로고    scopus 로고
    • Ab initio protein structure prediction of CASP III targets using ROSETTA
    • Simons, K.T., Bonneau, R., Ruczinski, I. & Baker, D. Ab initio protein structure prediction of CASP III targets using ROSETTA. Proteins (Suppl.) 3, 171-176 (1999).
    • (1999) Proteins (Suppl.) , vol.3 , pp. 171-176
    • Simons, K.T.1    Bonneau, R.2    Ruczinski, I.3    Baker, D.4
  • 40
    • 0032606133 scopus 로고    scopus 로고
    • Ab initio protein structure prediction using a combined hierarchical approach
    • Samudrala, R. Xia, Y. Huang, E. & Levitt, M. Ab initio protein structure prediction using a combined hierarchical approach. Proteins (Suppl.) 3, 194-198 (1999).
    • (1999) Proteins (Suppl.) , vol.3 , pp. 194-198
    • Samudrala, R.1    Xia, Y.2    Huang, E.3    Levitt, M.4
  • 41
    • 0032613288 scopus 로고    scopus 로고
    • Ab initio folding of proteins using restraints derived from evolutionary information
    • Ortiz, A. R., Kolinski, A., Rotkiewicz, P., Ilkowski, B. & Skolnick, J. Ab initio folding of proteins using restraints derived from evolutionary information. Proteins (Suppl.) 3, 177-185 (1999).
    • (1999) Proteins (Suppl.) , vol.3 , pp. 177-185
    • Ortiz, A.R.1    Kolinski, A.2    Rotkiewicz, P.3    Ilkowski, B.4    Skolnick, J.5
  • 42
    • 1542563746 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of E. coli DnaB helicase: Implications for structure rearrangements in the helicase hexamer
    • Weigelt, J., Brown, S. E., Miles, C. S. & Dixon, N. E. NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Structure 7, 681-690 (1999).
    • (1999) Structure , vol.7 , pp. 681-690
    • Weigelt, J.1    Brown, S.E.2    Miles, C.S.3    Dixon, N.E.4
  • 43
    • 0032514673 scopus 로고    scopus 로고
    • Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site
    • Slupsky, C. M. et al. Structure of the Ets-1 pointed domain and mitogen-activated protein kinase phosphorylation site. Proc. Natl Acad. Sci. USA 95, 12129-12134 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12129-12134
    • Slupsky, C.M.1
  • 44
    • 0032169864 scopus 로고    scopus 로고
    • A novel DNA-binding motif in MarA: The first structure for an AraC family transcriptional activator
    • Rhee, S., Martin, R. G., Rosner, J. L. & Davies, D. R. A novel DNA-binding motif in MarA: the first structure for an AraC family transcriptional activator. Proc. Natl Acad. Sci. USA 95, 10413-10418 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 10413-10418
    • Rhee, S.1    Martin, R.G.2    Rosner, J.L.3    Davies, D.R.4


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