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Volumn 120, Issue , 2002, Pages 35-76

Insights into specific problems in protein folding using simple concepts

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EID: 2242465042     PISSN: 00652385     EISSN: None     Source Type: Book Series    
DOI: 10.1002/0471224421.ch2     Document Type: Article
Times cited : (21)

References (128)
  • 3
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • C. B. Anfinsen, Principles that govern the folding of protein chains. Science 181, 223-230 (1973).
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 4
    • 0029866436 scopus 로고    scopus 로고
    • Why is protein folding so fast
    • R. L. Baldwin, Why is protein folding so fast. Proc. Natl. Acad. Sci. USA 93, 2627-2628 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2627-2628
    • Baldwin, R.L.1
  • 5
    • 0004062555 scopus 로고
    • P. Debrunner, J. C. M. Tsibris, and E. Munck, eds., University of Illinois Press, Urbana IL
    • C. Levinthal, in Mossbauer Spectroscopy in Biological Systems, P. Debrunner, J. C. M. Tsibris, and E. Munck, eds., University of Illinois Press, Urbana, IL, 1968.
    • (1968) Mossbauer Spectroscopy in Biological Systems
    • Levinthal, C.1
  • 6
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • K. A. Dill and H. S. Chan, From Levinthal to pathways to funnels. Natur. Struct. Biol. 4, 10-19 (1997).
    • (1997) Natur. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 7
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • A. R. Fersht, Nucleation mechanisms in protein folding. Curr. Opin. Struct. Biol. 7, 3-9 (1997).
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 10
    • 0033117927 scopus 로고    scopus 로고
    • Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models
    • D. Thirumalai and D. K. Klimov, Deciphering the timescales and mechanisms of protein folding using minimal off-lattice models. Curr. Opin. Struct. Biol. 9, 197-207 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 197-207
    • Thirumalai, D.1    Klimov, D.K.2
  • 11
    • 0032972986 scopus 로고    scopus 로고
    • Is protein folding hierarchic? I. Local structure and peptide folding
    • R. L. Baldwin and G. D. Rose, Is protein folding hierarchic? I. Local structure and peptide folding. Trends Biochem. Sci. 24, 26-33 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 26-33
    • Baldwin, R.L.1    Rose, G.D.2
  • 12
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • R. L. Baldwin and G. D. Rose, Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 24, 77-83 (1999).
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 14
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloids: What normal protein folding can tell us about fibrillogenesis and disease
    • P. T. Lansbury, Evolution of amyloids: What normal protein folding can tell us about fibrillogenesis and disease. Proc. Natl. Acad. Sci. USA 96, 3342-3344 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3342-3344
    • Lansbury, P.T.1
  • 16
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric λ repressor
    • G. S. Huang and T. G. Oas, Submillisecond folding of monomeric λ repressor. Proc. Natl. Acad. Sci. USA 92, 6878-6882 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 17
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism β-hairpin formation
    • V. Munoz, P. A. Thompson, J. Hofrichter, and W. A. Eaton, Folding dynamics and mechanism β-hairpin formation. Nature 390, 196-199 (1997).
    • (1997) Nature , vol.390 , pp. 196-199
    • Munoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 18
    • 0032921819 scopus 로고    scopus 로고
    • Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2
    • A. G. Ladurner and A. R. Fersht, Upper limit of the time scale for diffusion and chain collapse in chymotrypsin inhibitor 2. Nature Struct. Biol. 6, 28-31 (1999).
    • (1999) Nature Struct. Biol. , vol.6 , pp. 28-31
    • Ladurner, A.G.1    Fersht, A.R.2
  • 20
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • M. Rief, M. Gautel, F. Oesterhelt, J. M. Fernandez, and H. E. Gaub, Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276, 1109-1112 (1997).
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 21
    • 0031002460 scopus 로고    scopus 로고
    • Folding-unfolding transitions in single titin molecules characterized with laser tweezers
    • M. S. F. Kellermayer, S. B. Smith, H. L. Granzier, and C. Bustamante, Folding-unfolding transitions in single titin molecules characterized with laser tweezers. Science 276, 1112-1116 (1997).
    • (1997) Science , vol.276 , pp. 1112-1116
    • Kellermayer, M.S.F.1    Smith, S.B.2    Granzier, H.L.3    Bustamante, C.4
  • 25
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding
    • A. R. Fersht, Characterizing transition states in protein folding. Curr. Opin. Struct. Biol. 5, 79-84 (1995).
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 79-84
    • Fersht, A.R.1
  • 26
    • 0028868995 scopus 로고
    • The nature of the transition state of chymotrypsin inhibitor 2 analyzed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • L. S. Itzhaki, D. E. Otzen, and A. R. Fersht, The nature of the transition state of chymotrypsin inhibitor 2 analyzed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254, 260-288 (1995).
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 27
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of β-hairpin in protein G folding
    • E. L. McCallister, E. Alm, and D. Baker, Critical role of β-hairpin in protein G folding. Natur. Struct. Biol. 7, 669-673 (2000).
    • (2000) Natur. Struct. Biol. , Issue.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 28
    • 0031815749 scopus 로고    scopus 로고
    • How do small single domain proteins fold
    • S. E. Jackson, How do small single domain proteins fold. Fold. Des. 3, R81-R91 (1998).
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 30
    • 0028270634 scopus 로고
    • Kinetics of protein folding: A lattice model study of the requirements for folding to the native state
    • A. Sali, E. Shakhnovich, and M. Karplus, Kinetics of protein folding: A lattice model study of the requirements for folding to the native state. J. Mol. Biol. 235, 1614-1636 (1994).
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Sali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 34
    • 0001337986 scopus 로고    scopus 로고
    • Linking rates of folding in lattice models of proteins with underlying thermodynamic characteristics
    • D. K. Klimov and D. Thirumalai, Linking rates of folding in lattice models of proteins with underlying thermodynamic characteristics. J. Chem. Phys. 109, 4119-4125 (1998).
    • (1998) J. Chem. Phys. , vol.109 , pp. 4119-4125
    • Klimov, D.K.1    Thirumalai, D.2
  • 36
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity of protein folding
    • D. Baker, A surprising simplicity of protein folding. Nature 405, 39-42 (2000).
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 37
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • K. Plaxco, K. T. Simons, and D. Baker, 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.1    Simons, K.T.2    Baker, D.3
  • 38
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of immunoglobulin-like β-sandwich proteins suggest that they share a common folding pathway
    • J. Clarke, E. Cota, S. B. Fowler, and S. J. Hamill, Folding studies of immunoglobulin-like b-sandwich proteins suggest that they share a common folding pathway. Struct. Fold. Des. 7, 1145-1153 (1999).
    • (1999) Struct. Fold. Des. , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.J.4
  • 40
    • 0000050196 scopus 로고
    • From minimal models to real proteins: Time scales for protein folding
    • D. Thirumalai, From minimal models to real proteins: Time scales for protein folding. J. Phys. I 5, 1457-1467, 1995.
    • (1995) J. Phys. I , vol.5 , pp. 1457-1467
    • Thirumalai, D.1
  • 41
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • A. R. Dinner,A. Sali, L. J. Smith, C. M. Dobson, and M. Karplus, Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem. Sci. 25, 331-339 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 42
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1- microsecond simulation in aqueous solution
    • Y. Duan and P. A. Kollman, Pathways to a protein folding intermediate observed in a 1- microsecond simulation in aqueous solution. Science 282, 740-744 (1998).
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 43
    • 0343418251 scopus 로고    scopus 로고
    • Exploring the folding mechanisms using lattice models
    • P. Grassberger, G. T. Barkema, and W. Nadler, eds., Singapore, World Scientific
    • D. Thirumalai, D. K. Klimov, and M. R. Betancourt, Exploring the folding mechanisms using lattice models, in Monte Carlo Approach to Biopolymers and Protein Folding, P. Grassberger, G. T. Barkema, and W. Nadler, eds., Singapore, World Scientific, 1998, pp. 19-28.
    • (1998) Monte Carlo Approach to Biopolymers and Protein Folding , pp. 19-28
    • Thirumalai, D.1    Klimov, D.K.2    Betancourt, M.R.3
  • 44
    • 0008451197 scopus 로고    scopus 로고
    • Emergence of stable and fast folding protein structures
    • in S. Kim, K. J. Lee, andW. Sung, eds., American Institute of Physics, New York
    • D. Thirumalai and D. K. Klimov, Emergence of stable and fast folding protein structures, in S. Kim, K. J. Lee, andW. Sung, eds., Stochastic Dynamics and Pattern Formation in Biological Systems, American Institute of Physics, New York, 2000, pp. 95-111.
    • (2000) Stochastic Dynamics and Pattern Formation in Biological Systems , pp. 95-111
    • Thirumalai, D.1    Klimov, D.K.2
  • 45
    • 0028941444 scopus 로고
    • Theoretical predictions of folding pathways using the proximity rule with applications to BPTI
    • C. Camacho and D. Thirumalai, Theoretical predictions of folding pathways using the proximity rule with applications to BPTI. Proc. Natl. Acad. Sci. USA 92, 1277-1281 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1277-1281
    • Camacho, C.1    Thirumalai, D.2
  • 46
    • 0029028698 scopus 로고
    • Modeling the role of disulfide bonds in protein folding: Entropic barriers and pathways
    • C. Camacho and D. Thirumalai, Modeling the role of disulfide bonds in protein folding: Entropic barriers and pathways. Proteins Struct. Funct. Gen. 22, 27-40 (1995).
    • (1995) Proteins Struct. Funct. Gen. , vol.22 , pp. 27-40
    • Camacho, C.1    Thirumalai, D.2
  • 47
    • 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, 627-644 (1999).
    • (1999) J. Mol. Biol. , vol.287 , pp. 627-644
    • Betancourt, M.R.1    Thirumalai, D.2
  • 48
    • 0003101252 scopus 로고
    • Statistical treatment of polymer solutions at infinite dilution
    • W. J. C. Orr, Statistical treatment of polymer solutions at infinite dilution. Trans. Faraday Soc. 43, 12-27 (1947).
    • (1947) Trans. Faraday Soc. , vol.43 , pp. 12-27
    • Orr, W.J.C.1
  • 49
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding, and fluctuations by computer simulation
    • H. Taketomi, Y. Ueda, and N. Gō, Studies on protein folding, unfolding, and fluctuations by computer simulation. Int. J. Pept. Protein Res. 7, 445-459 (1975).
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Go, N.3
  • 50
    • 36549094651 scopus 로고
    • Intrachain loops in polymers: Effects of excluded volume
    • H. S. Chan and K. A. Dill, Intrachain loops in polymers: Effects of excluded volume. J. Chem. Phys. 90, 493-509 (1989).
    • (1989) J. Chem. Phys. , vol.90 , pp. 493-509
    • Chan, H.S.1    Dill, K.A.2
  • 51
    • 0001669870 scopus 로고
    • Kinetic and thermodynamic analysis of protein-like heteropolymers: Monte carlo histogram technique
    • N. D. Socci and J. N. Onuchic, Kinetic and thermodynamic analysis of protein-like heteropolymers: Monte carlo histogram technique. J. Chem. Phys. 103, 4732-4744 (1995).
    • (1995) J. Chem. Phys. , vol.103 , pp. 4732-4744
    • Socci, N.D.1    Onuchic, J.N.2
  • 52
    • 0028024928 scopus 로고
    • Specific nucleus as the transition state for protein folding: Evidence from the lattice model
    • V. I. Abkevich, A. M. Gutin, and E. I. Shakhnovich, 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.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 53
    • 33845377127 scopus 로고
    • Estimation of effective inter-residue contact energies from protein crystal structures: Quasi-chemical approximation
    • S. Miyazawa and R. L. Jernigan, Estimation of effective inter-residue contact energies from protein crystal structures: Quasi-chemical approximation. Macromolecules 18, 534-552 (1985).
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 54
    • 0000778903 scopus 로고
    • A general method for the prediction of the three dimensional structure and folding pathway of globular proteins: Application to designed helical proteins
    • A. Kolinski, A. Godzik, and J. Skolnick, A general method for the prediction of the three dimensional structure and folding pathway of globular proteins: Application to designed helical proteins. J. Chem. Phys. 98, 7420-7433 (1993).
    • (1993) J. Chem. Phys. , vol.98 , pp. 7420-7433
    • Kolinski, A.1    Godzik, A.2    Skolnick, J.3
  • 55
    • 0033005899 scopus 로고    scopus 로고
    • Pair potentials for protein folding: Choice of reference states and sensitivity of predicted native states to variations in the interaction schemes
    • M. R. Betancourt and D. Thirumalai, Pair potentials for protein folding: Choice of reference states and sensitivity of predicted native states to variations in the interaction schemes. Prot. Sci. 8, 1-8 (1999).
    • (1999) Prot. Sci. , vol.8 , pp. 1-8
    • Betancourt, M.R.1    Thirumalai, D.2
  • 56
    • 0030596063 scopus 로고    scopus 로고
    • How to derive a protein folding potential? A new approach to an old problem
    • L. A. Mirny and E. I. Shakhnovich, How to derive a protein folding potential? A new approach to an old problem. J. Mol. Biol. 264, 1164-1179 (1996).
    • (1996) J. Mol. Biol. , vol.264 , pp. 1164-1179
    • Mirny, L.A.1    Shakhnovich, E.I.2
  • 57
    • 0034308163 scopus 로고    scopus 로고
    • Distance-dependent, pair potential for protein folding: Results from linear optimization
    • D. Tobi and R. Elber, Distance-dependent, pair potential for protein folding: Results from linear optimization. Proteins Struct. Funct. Gen. 41, 40-46 (2000).
    • (2000) Proteins Struct. Funct. Gen. , vol.41 , pp. 40-46
    • Tobi, D.1    Elber, R.2
  • 58
    • 0020972782 scopus 로고
    • Theoretical studies of protein folding
    • N. Gō, 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
  • 59
    • 0034705115 scopus 로고    scopus 로고
    • How native-state topology affects the folding of dihydrofolate reductase and interleukin-1
    • C. Clementi, P. A. Jennings, and J. N. Onuchic, How native-state topology affects the folding of dihydrofolate reductase and interleukin-1. Proc. Natl. Acad. Sci. USA 97, 5871-5876 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5871-5876
    • Clementi, C.1    Jennings, P.A.2    Onuchic, J.N.3
  • 60
    • 0001504441 scopus 로고    scopus 로고
    • Cooperativity in protein folding: From lattice models with side chains to real proteins
    • D. K. Klimov and D. Thirumalai, Cooperativity in protein folding: From lattice models with side chains to real proteins. Fold. Des. 3, 127-139 (1998).
    • (1998) Fold. Des. , vol.3 , pp. 127-139
    • Klimov, D.K.1    Thirumalai, D.2
  • 61
    • 12644275369 scopus 로고
    • Computer enumerations
    • C. Domb and M.S. Green, eds., Academic Press, New York
    • J. L. Martin, Computer enumerations, in Phase Transitions and Critical Phenomena, C. Domb and M.S. Green, eds., Academic Press, New York, 1974, pp. 102-110.
    • (1974) Phase Transitions and Critical Phenomena , pp. 102-110
    • Martin, J.L.1
  • 63
    • 33646987405 scopus 로고
    • Optimized monte carlo data analysis
    • A. M. Ferrenberg and R. H. Swendsen, Optimized monte carlo data analysis. Phys. Rev. Lett. 63, 1195-1198 (1989).
    • (1989) Phys. Rev. Lett. , vol.63 , pp. 1195-1198
    • Ferrenberg, A.M.1    Swendsen, R.H.2
  • 64
    • 0033730431 scopus 로고    scopus 로고
    • The flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding
    • R. V. Pappu, R. Srinivasan, and G. D. Rose, The flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding. Proc. Natl. Acad. Sci. USA 97, 12565-12570 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12565-12570
    • Pappu, R.V.1    Srinivasan, R.2    Rose, G.D.3
  • 65
    • 0030601851 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of folding of a de novo designed fourhelix bundle
    • Z. Guo and D. Thirumalai, Kinetics and thermodynamics of folding of a de novo designed fourhelix bundle. J. Mol. Biol. 263, 323-343 (1996).
    • (1996) J. Mol. Biol. , vol.263 , pp. 323-343
    • Guo, Z.1    Thirumalai, D.2
  • 67
    • 0029772552 scopus 로고    scopus 로고
    • Emergence of preferred structures in a simple model of protein folding
    • H. Li, N. Wingreen, and C. Tang, Emergence of preferred structures in a simple model of protein folding. Science 273, 666-669 (1996).
    • (1996) Science , vol.273 , pp. 666-669
    • Li, H.1    Wingreen, N.2    Tang, C.3
  • 68
    • 0029952910 scopus 로고    scopus 로고
    • Symmetry and the energy landscape of biomolecules
    • P. G.Wolynes, Symmetry and the energy landscape of biomolecules. Proc. Natl. Acad. Sci. USA 93, 14249-14255 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14249-14255
    • Wolynes, P.G.1
  • 69
    • 0037825814 scopus 로고    scopus 로고
    • Magic numbers in protein structures
    • Per-Anker Lindgard and H. Bohr, Magic numbers in protein structures. Phys. Rev. Lett. 77, 779-782 (1996).
    • (1996) Phys. Rev. Lett. , vol.77 , pp. 779-782
    • Lindgard, P.-A.1    Bohr, H.2
  • 71
    • 0035895436 scopus 로고    scopus 로고
    • Apparent two-state tendamistat folding is a sequential process along a defined pathway
    • A. Bachman and T. Kiefhaber, Apparent two-state tendamistat folding is a sequential process along a defined pathway. J. Mol. Biol. 306, 375-386 (2001).
    • (2001) J. Mol. Biol. , vol.306 , pp. 375-386
    • Bachman, A.1    Kiefhaber, T.2
  • 72
    • 0033574069 scopus 로고    scopus 로고
    • Folding pathway of a lattice model for proteins
    • V. S. Pande and D. S. Rokhsar, Folding pathway of a lattice model for proteins. Proc. Natl. Acad. Sci. USA 96, 1273-1278 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1273-1278
    • Pande, V.S.1    Rokhsar, D.S.2
  • 73
    • 0029010695 scopus 로고
    • Kinetics of protein folding: Nucleation mechanism, time scales and pathways
    • Z. Guo and D. Thirumalai, Kinetics of protein folding: Nucleation mechanism, time scales and pathways. Biopolymers, 36, 83-103 (1995).
    • (1995) Biopolymers , vol.36 , pp. 83-103
    • Guo, Z.1    Thirumalai, D.2
  • 74
    • 0029025915 scopus 로고
    • Kinetic traps in lysozyme folding
    • T. Kiefhaber, Kinetic traps in lysozyme folding. Proc. Natl. Acad. Sci. USA 92, 9029-9033 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9029-9033
    • Kiefhaber, T.1
  • 75
    • 0030669671 scopus 로고    scopus 로고
    • Intermediates and kinetic traps in the folding of large ribozyme revealed by UVand CD spectroscopies and catalytic activity
    • T. Pan and T. R. Sosnick, Intermediates and kinetic traps in the folding of large ribozyme revealed by UVand CD spectroscopies and catalytic activity. Nature Struct. Biol. 14, 931-938 (1997).
    • (1997) Nature Struct. Biol. , vol.14 , pp. 931-938
    • Pan, T.1    Sosnick, T.R.2
  • 76
    • 0031576990 scopus 로고    scopus 로고
    • Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process
    • A. Matagne, S. E. Radford, and C. M. Dobson, Fast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process. J. Mol. Biol. 267, 1068-1074 (1997).
    • (1997) J. Mol. Biol. , vol.267 , pp. 1068-1074
    • Matagne, A.1    Radford, S.E.2    Dobson, C.M.3
  • 77
    • 0034674420 scopus 로고    scopus 로고
    • A single-molecule study of RNA catalysis and folding
    • DOI 10.1126/science.288.5473.2048
    • X. Zhuang, L. E. Bartley, A. P. Babcock, R. Russell, T. Ha, D. Herschlag, and S. Chu, A singlemolecule study of RNA catalysis and folding. Science 288, 2048-2051 (2000). (Pubitemid 30397686)
    • (2000) Science , vol.288 , Issue.5473 , pp. 2048-2051
    • Zhuang, X.1    Bartley, L.E.2    Babcock, H.P.3    Russell, R.4    Ha, T.5    Herschlag, D.6    Chu, S.7
  • 78
    • 0141448394 scopus 로고    scopus 로고
    • Kinetic partitioning as a unifying theme in the folding of biomolecules
    • D. Thirumalai, D. K. Klimov, and S. A. Woodson, Kinetic partitioning as a unifying theme in the folding of biomolecules. Theor. Chem. Acc. 1, 149-156 (1997).
    • (1997) Theor. Chem. Acc. , vol.1 , pp. 149-156
    • Thirumalai, D.1    Klimov, D.K.2    Woodson, S.A.3
  • 79
    • 0016277150 scopus 로고
    • Renaturation of the reduced bovine pancreatic trypsin inhibitor
    • T. E. Creighton, Renaturation of the reduced bovine pancreatic trypsin inhibitor. J. Mol. Biol. 87, 563-577 (1974).
    • (1974) J. Mol. Biol. , vol.87 , pp. 563-577
    • Creighton, T.E.1
  • 80
    • 0017389755 scopus 로고
    • Conformational restrictions on the pathway of folding and unfolding of BPTI
    • T. E. Creighton, Conformational restrictions on the pathway of folding and unfolding of BPTI. J. Mol. Biol. 113, 275-293 (1977).
    • (1977) J. Mol. Biol. , vol.113 , pp. 275-293
    • Creighton, T.E.1
  • 81
    • 0017392811 scopus 로고
    • Energetics of folding and unfolding of pancreatic trypsin inhibitor
    • T. E. Creighton, Energetics of folding and unfolding of pancreatic trypsin inhibitor. J. Mol. Biol. 113, 295-312 (1977).
    • (1977) J. Mol. Biol. , vol.113 , pp. 295-312
    • Creighton, T.E.1
  • 82
    • 0017401942 scopus 로고
    • Effects of urea and guanidine. Hcl on the folding and unfolding of pancreatic trypsin inhibitor
    • T. E. Creighton, Effects of urea and guanidine. Hcl on the folding and unfolding of pancreatic trypsin inhibitor. J. Mol. Biol. 113, 313-328 (1977).
    • (1977) J. Mol. Biol. , vol.113 , pp. 313-328
    • Creighton, T.E.1
  • 83
    • 0021659707 scopus 로고
    • Kinetic role of meta-stable native like two disulphide species in the folding transition of bovine pancreatic trypsin inhibitor
    • T. E. Creighton and D. P. Goldenberg, Kinetic role of meta-stable native like two disulphide species in the folding transition of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 179, 497-526 (1984).
    • (1984) J. Mol. Biol. , vol.179 , pp. 497-526
    • Creighton, T.E.1    Goldenberg, D.P.2
  • 84
    • 0025949415 scopus 로고
    • Reexamination of the folding of BPTI: Predominance of native intermediates
    • J. S. Weissman and P. S. Kim, Reexamination of the folding of BPTI: Predominance of native intermediates. Science 253, 1386-1393 (1991).
    • (1991) Science , vol.253 , pp. 1386-1393
    • Weissman, J.S.1    Kim, P.S.2
  • 85
    • 0026666246 scopus 로고
    • Kinetic role of non-native species in the folding of bovine pancreatic trypsin inhibitor
    • J. S. Weissman and P. S. Kim, Kinetic role of non-native species in the folding of bovine pancreatic trypsin inhibitor. Proc. Nat. Acad. Sci. USA 89, 9900-9904 (1992).
    • (1992) Proc. Nat. Acad. Sci. USA , vol.89 , pp. 9900-9904
    • Weissman, J.S.1    Kim, P.S.2
  • 86
    • 0026476393 scopus 로고
    • The pro region of BPTI facilitates folding
    • J. S. Weissman and P. S. Kim, The pro region of BPTI facilitates folding. Cell 71, 841-851 (1992).
    • (1992) Cell , vol.71 , pp. 841-851
    • Weissman, J.S.1    Kim, P.S.2
  • 87
    • 0027270735 scopus 로고
    • Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase
    • J. S.Weissman and P. S. Kim, Efficient catalysis of disulphide bond rearrangements by protein disulphide isomerase. Nature 365, 185-188 (1993).
    • (1993) Nature , vol.365 , pp. 185-188
    • Weissman, J.S.1    Kim, P.S.2
  • 88
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • C. B. Anfinsen, Principles that govern the folding of protein chains. Science 181, 223-230 (1973).
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 89
    • 0000114379 scopus 로고    scopus 로고
    • Time scales for the formation of the most probable tertiary contacts in proteins with applications to cytochrome C
    • D. Thirumalai, Time scales for the formation of the most probable tertiary contacts in proteins with applications to cytochrome C. J. Phys. Chem. 103, 608-610 (1999).
    • (1999) J. Phys. Chem. , vol.103 , pp. 608-610
    • Thirumalai, D.1
  • 90
    • 0034646218 scopus 로고    scopus 로고
    • Mechanisms and kinetics of β-hairpin formation
    • D. K. Klimov and D. Thirumalai, Mechanisms and kinetics of β-hairpin formation. Proc. Natl. Acad. Sci. USA 97, 2544-2549 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2544-2549
    • Klimov, D.K.1    Thirumalai, D.2
  • 91
    • 0027255302 scopus 로고
    • Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor-forming 1st disulphide bonds in analogues of the reduced protein
    • N. J. Darby and T. E. Creighton, Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor-forming 1st disulphide bonds in analogues of the reduced protein. J. Mol. Biol. 232, 873-886 (1993).
    • (1993) J. Mol. Biol. , vol.232 , pp. 873-886
    • Darby, N.J.1    Creighton, T.E.2
  • 92
    • 0029098928 scopus 로고
    • A third native one-disulphide intermediate in the folding of bovine pancreatic trypsin inhibitor
    • M. Dadlez and P. S. Kim, A third native one-disulphide intermediate in the folding of bovine pancreatic trypsin inhibitor. Nature Struct. Biol. 2, 674-679 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 674-679
    • Dadlez, M.1    Kim, P.S.2
  • 93
    • 0028966372 scopus 로고
    • Partially folded molten globule and molten coil states of bovine pancreatic trypsin inhibitor
    • M. Ferrer, G. Barany, and C.Woodward, Partially folded molten globule and molten coil states of bovine pancreatic trypsin inhibitor. Nature Struct. Biol. 2, 211-217 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 211-217
    • Ferrer, M.1    Barany, G.2    Woodward, C.3
  • 94
    • 0027723275 scopus 로고
    • Amino acid replacement that eliminates kinetic traps in the folding pathway of pancreatic trypsin inhibitor
    • J. X. Zhang and D. P. Goldenberg, Amino acid replacement that eliminates kinetic traps in the folding pathway of pancreatic trypsin inhibitor. Biochemistry 32, 14075-14081 (1993).
    • (1993) Biochemistry , vol.32 , pp. 14075-14081
    • Zhang, J.X.1    Goldenberg, D.P.2
  • 95
    • 0027155577 scopus 로고
    • Engineered disulfide bonds as probes of the folding pathway of barnase-increasing the stability of proteins against the rate of denaturation
    • J. Clarke and A. R. Fersht, Engineered disulfide bonds as probes of the folding pathway of barnase-increasing the stability of proteins against the rate of denaturation. Biochemistry 32, 4322-4329 (1993).
    • (1993) Biochemistry , vol.32 , pp. 4322-4329
    • Clarke, J.1    Fersht, A.R.2
  • 96
    • 0034697986 scopus 로고    scopus 로고
    • What can disulfide bonds tell us about protein energetics, function and folding: Simulations and bioinformatic analysis
    • V. I. Abkevich and E. I. Shakhnovich. What can disulfide bonds tell us about protein energetics, function and folding: Simulations and bioinformatic analysis. J. Mol. Biol. 300, 975-985 (2000).
    • (2000) J. Mol. Biol. , vol.300 , pp. 975-985
    • Abkevich, V.I.1    Shakhnovich, E.I.2
  • 97
    • 0030050614 scopus 로고    scopus 로고
    • A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo
    • G. H. Lorimer, A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo. FASEB J. 10, 5-9 (1996).
    • (1996) FASEB J. , vol.10 , pp. 5-9
    • Lorimer, G.H.1
  • 99
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • W. A. Fenton and A. L. Horwich, GroEL-mediated protein folding. Prot. Sci. 6, 743-760 (1997).
    • (1997) Prot. Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 100
    • 0030766287 scopus 로고    scopus 로고
    • Folding with a two-stroke motor
    • G. H. Lorimer, Folding with a two-stroke motor. Nature 388, 720-723 (1997).
    • (1997) Nature , vol.388 , pp. 720-723
    • Lorimer, G.H.1
  • 101
    • 0032464019 scopus 로고    scopus 로고
    • GroEL/GroES: Structure and function of a two-stroke folding machine
    • Z. Xu and P. B. Sigler, GroEL/GroES: Structure and function of a two-stroke folding machine. J. Struct. Biol. 124, 129-141 (1999).
    • (1999) J. Struct. Biol. , vol.124 , pp. 129-141
    • Xu, Z.1    Sigler, P.B.2
  • 103
    • 0002617993 scopus 로고    scopus 로고
    • A simple model of chaperonin-mediated protein folding
    • H. S. Chan and K. A. Dill, A simple model of chaperonin-mediated protein folding. Prot. Struct. Funct. Genet. 24, 345-351 (1996).
    • (1996) Prot. Struct. Funct. Genet. , vol.24 , pp. 345-351
    • Chan, H.S.1    Dill, K.A.2
  • 104
    • 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, 4030-4035 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4030-4035
    • Todd, M.J.1    Lorimer, G.H.2    Thirumalai, D.3
  • 105
    • 0029664316 scopus 로고    scopus 로고
    • Toward a mechanism of GroEL-GroES chaperone activity: An ATPase-gated and pulsed folding and annealing cage
    • F. J. Corrales and A. R. Fersht, Toward a mechanism of GroEL-GroES chaperone activity: An ATPase-gated and pulsed folding and annealing cage. Proc. Natl. Acad. Sci. USA 93, 4509-4512 (1996).
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4509-4512
    • Corrales, F.J.1    Fersht, A.R.2
  • 107
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8Å resolution
    • J. F. Hunt, A. J. Weaver, S. J. Landry, L. Gierasch, and J. Deisenhofer, The crystal structure of the GroES co-chaperonin at 2.8Å resolution. Nature 379, 37-49 (1996).
    • (1996) Nature , vol.379 , pp. 37-49
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.J.3    Gierasch, L.4    Deisenhofer, J.5
  • 108
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES- (ADP)7 chaperonin complex
    • Z. Xu, A. Horwich, and P. B. Sigler, The crystal structure of the asymmetric GroEL-GroES- (ADP)7 chaperonin complex. Nature 388, 741-750 (1997).
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.2    Sigler, P.B.3
  • 109
    • 0034665864 scopus 로고    scopus 로고
    • A dynamic model for allosteric mechanism for GroEL
    • J. Ma, P. B. Sigler, Z. H. Xu, and M. Karplus, A dynamic model for allosteric mechanism for GroEL. J. Mol. Biol. 302, 303-313 (2000).
    • (2000) J. Mol. Biol. , vol.302 , pp. 303-313
    • Ma, J.1    Sigler, P.B.2    Xu, Z.H.3    Karplus, M.4
  • 110
    • 0029004759 scopus 로고
    • Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
    • O. Yifrach and A. Horovitz, Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL. Biochemistry 34, 5303-5308 (1995).
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horovitz, A.2
  • 112
    • 0027065105 scopus 로고
    • Purified chaperonin 60 (GroEL) interacts with the non-native states of a multitude of Escherichia coli proteins
    • P. V. Viitanen, A. A. Gatenby, and G. H. Lorimer, Purified chaperonin 60 (GroEL) interacts with the non-native states of a multitude of Escherichia coli proteins. Prot. Sci. 1, 363-369 (1992).
    • (1992) Prot. Sci. , vol.1 , pp. 363-369
    • Viitanen, P.V.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 113
    • 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, 757-768 (1999).
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 114
    • 0033543656 scopus 로고    scopus 로고
    • GroEL recognizes sequential and nonsequential linear structural motifs compatible with extended β-strands and α-helices
    • J. Chatellier, A. M. Buckle, and A. R. Fersht, GroEL recognizes sequential and nonsequential linear structural motifs compatible with extended β-strands and α-helices. J. Mol. Biol. 292, 163-172 (1999).
    • (1999) J. Mol. Biol. , vol.292 , pp. 163-172
    • Chatellier, J.1    Buckle, A.M.2    Fersht, A.R.3
  • 116
    • 0028023724 scopus 로고
    • Statistical mechanics of kinetic proof reading in protein folding in vivo
    • K. Gulukota and P. G.Wolynes, Statistical mechanics of kinetic proof reading in protein folding in vivo. Proc. Natl. Acad. Sci. USA 91, 9292-9296 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9292-9296
    • Gulukota, K.1    Wolynes, P.G.2
  • 117
    • 0034652350 scopus 로고    scopus 로고
    • Coupling between protein folding and allostery in the GroE chaperonin system
    • O. Yifrach and A. Horovitz, Coupling between protein folding and allostery in the GroE chaperonin system. Proc. Natl. Acad. Sci. 97, 1521-1524 (2000).
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 1521-1524
    • Yifrach, O.1    Horovitz, A.2
  • 118
    • 78651189765 scopus 로고
    • On the nature of allosteric interactions: A plausible model
    • J. Monod, J. Wyman, and J. P. Changeaux, On the nature of allosteric interactions: A plausible model. J. Mol. Biol. 12, 88-118 (1965).
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeaux, J.P.3
  • 119
    • 0030061845 scopus 로고    scopus 로고
    • Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
    • R. Zahn, S. Perrett, G. Stenberg, and A. R. Fersht, Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science 271, 642-645 (1996).
    • (1996) Science , vol.271 , pp. 642-645
    • Zahn, R.1    Perrett, S.2    Stenberg, G.3    Fersht, A.R.4
  • 120
    • 0031554905 scopus 로고    scopus 로고
    • Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR
    • S. E. Nieba-Axmann, M. Ottinger, K. Wuthrich, and A. Pluckthun, Multiple cycles of global unfolding of GroEL-bound cyclophilin A evidenced by NMR. J. Mol. Biol. 271, 803-818 (1997).
    • (1997) J. Mol. Biol. , vol.271 , pp. 803-818
    • Nieba-Axmann, S.E.1    Ottinger, M.2    Wuthrich, K.3    Pluckthun, A.4
  • 121
    • 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, 822-825 (1999).
    • (1999) Science , vol.284 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 122
    • 0033817704 scopus 로고    scopus 로고
    • Stretching single molecules into novel conformations using the atomic force microscope
    • T. E. Fisher, P. E. Marszalek, and J. M. Fernandez, Stretching single molecules into novel conformations using the atomic force microscope. Nat. Struct. Biol. 9, 719-724 (2000).
    • (2000) Nat. Struct. Biol. , vol.9 , pp. 719-724
    • Fisher, T.E.1    Marszalek, P.E.2    Fernandez, J.M.3
  • 123
    • 0034691149 scopus 로고    scopus 로고
    • Native topology determines force-induced unfolding pathways in globular proteins
    • D. K. Klimov and D. Thirumalai, Native topology determines force-induced unfolding pathways in globular proteins. Proc. Natl. Acad. Sci. USA 97, 7254-7259 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7254-7259
    • Klimov, D.K.1    Thirumalai, D.2
  • 127
    • 0029119568 scopus 로고
    • Rasmol: Biomolecular graphics for all
    • R. Sayle and E. J. Milner-White, Rasmol: Biomolecular graphics for all. Trends Biochem. Sci. 20, 374-376 (1995).
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 374-376
    • Sayle, R.1    Milner-White, E.J.2
  • 128
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • W. A. Fenton, Y. Kashi, K. Furtak, and A. L. Horwich, Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371, 614-619 (1994).
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4


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