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Volumn 3, Issue 6, 1996, Pages 425-432

Fast-folding experiments and the topography of protein folding energy landscapes

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL MODEL; PROTEIN FOLDING; REVIEW;

EID: 0030155292     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(96)90090-3     Document Type: Review
Times cited : (95)

References (39)
  • 1
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P.S. & Baldwin, R.L. (1990). Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59, 631-660.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 2
    • 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. (1995). Funnels, pathways and the energy landscape of protein folding: a synthesis. Proteins 21, 167-195.
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 3
    • 0345263026 scopus 로고
    • Molecular dynamics of associative memory Hamiltonians for protein tertiary structure recognition
    • Friedrichs, M. & Wolynes, P.G. (1990). Molecular dynamics of associative memory Hamiltonians for protein tertiary structure recognition. Tetrahedron (Comp. Meth) 3, 175-190.
    • (1990) Tetrahedron (Comp. Meth) , vol.3 , pp. 175-190
    • Friedrichs, M.1    Wolynes, P.G.2
  • 4
    • 0028929556 scopus 로고
    • Principles of protein folding: A perspective from simple exact models
    • Dill, K.A., et al., & Chan, H.S. (1995). Principles of protein folding: a perspective from simple exact models. Protein Sci. 4, 561-602.
    • (1995) Protein Sci. , vol.4 , pp. 561-602
    • Dill, K.A.1    Chan, H.S.2
  • 5
    • 0026643094 scopus 로고
    • The nature of the folded state of globular proteins
    • Honeycutt, J.D. & Thirumalai, D. (1992). The nature of the folded state of globular proteins. Biopolymers 32, 695-709.
    • (1992) Biopolymers , vol.32 , pp. 695-709
    • Honeycutt, J.D.1    Thirumalai, D.2
  • 6
    • 0028270634 scopus 로고
    • Kinetics of protein folding: A lattice model study of the requirements for folding to the native state
    • Sali, A., Shakhnovich, E. & Karplus, M. (1994). Kinetics of protein folding: a lattice model study of the requirements for folding to the native state. J. Mol. Biol. 235, 1614-1636.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1614-1636
    • Sali, A.1    Shakhnovich, E.2    Karplus, M.3
  • 7
    • 0007725036 scopus 로고
    • Folding kinetics of protein-like heteropolymers
    • Socci, N.D. & Onuchic, J.N. (1994). Folding kinetics of protein-like heteropolymers. J. Chem. Phys. 101, 1519-1528.
    • (1994) J. Chem. Phys. , vol.101 , pp. 1519-1528
    • Socci, N.D.1    Onuchic, J.N.2
  • 8
    • 0001669870 scopus 로고
    • Kinetic and thermodynamic analysis of protein-like heteropolymers: Monte Carlo histogram technique
    • Socci, N.D. & Onuchic, J.N. (1995). Kinetic and thermodynamic analysis of protein-like heteropolymers: Monte Carlo histogram technique. J. Chem. Phys. 103, 4732-4744.
    • (1995) J. Chem. Phys. , vol.103 , pp. 4732-4744
    • Socci, N.D.1    Onuchic, J.N.2
  • 9
    • 0027131947 scopus 로고
    • Fast events in protein folding initiated by nanosecond laser photolysis
    • Jones, C.M., et al., & Eaton, W.A. (1993). Fast events in protein folding initiated by nanosecond laser photolysis. Proc. Natl. Acad. Sci. USA 90, 11860-11864.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11860-11864
    • Jones, C.M.1    Eaton, W.A.2
  • 11
    • 0030046906 scopus 로고    scopus 로고
    • Fast events in protein folding, helix melting and formation in a small peptide
    • Williams, S., et al., & Dyer, R.B. (1996). Fast events in protein folding, helix melting and formation in a small peptide. Biochemistry 36, 691-698.
    • (1996) Biochemistry , vol.36 , pp. 691-698
    • Williams, S.1    Dyer, R.B.2
  • 12
    • 0030584652 scopus 로고    scopus 로고
    • Protein folding triggered by electron transfer
    • Pascher, T., Chesick, J.P., Winkler, J.R. & Gray, H.B. (1996). Protein folding triggered by electron transfer. Science 271, 1558-1560.
    • (1996) Science , vol.271 , pp. 1558-1560
    • Pascher, T.1    Chesick, J.P.2    Winkler, J.R.3    Gray, H.B.4
  • 13
    • 0029973119 scopus 로고    scopus 로고
    • Direct observation of fast protein folding: The initial collapse of apomyoglobin
    • Ballew, R.M., Sabelko, J. & Gruebele, M. (1996). Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proc. Natl. Acad. USA 93, 5759-5764.
    • (1996) Proc. Natl. Acad. USA , vol.93 , pp. 5759-5764
    • Ballew, R.M.1    Sabelko, J.2    Gruebele, M.3
  • 14
    • 0029151158 scopus 로고
    • Submillisecond folding of monomeric λ represser
    • Huang, G.S. & Oas, T.G. (1995). Submillisecond folding of monomeric λ represser. Proc. Natl. Acad. Sci. USA 92, 6878-6882.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6878-6882
    • Huang, G.S.1    Oas, T.G.2
  • 16
    • 0030582432 scopus 로고    scopus 로고
    • Hydrogen exchange kinetics in the cold denatured state of ribonuclease A
    • in press
    • Nash, D., Lee, B. & Jonas, J. (1996). Hydrogen exchange kinetics in the cold denatured state of ribonuclease A. Biochim. Biophys. Acta, in press.
    • (1996) Biochim. Biophys. Acta
    • Nash, D.1    Lee, B.2    Jonas, J.3
  • 17
    • 0002775727 scopus 로고
    • Early stages of protein folding
    • (Pain, R.H., ed.), Oxford Press, Oxford
    • Roder, H. & Elove, G.A. (1994). Early stages of protein folding. In Mechanisms of Protein Folding. (Pain, R.H., ed.), pp. 26-54, Oxford Press, Oxford.
    • (1994) Mechanisms of Protein Folding , pp. 26-54
    • Roder, H.1    Elove, G.A.2
  • 18
    • 0027536094 scopus 로고
    • Structure and dynamics of the acid-denatured molten globule state of a-lactalbumin: A two-dimensional NMR study
    • Alexandrescu, A.T., Evans, P.A., Pitkeathly, M., Baum, J. & Dobson, C.M. (1993). Structure and dynamics of the acid-denatured molten globule state of a-lactalbumin: a two-dimensional NMR study. Biochemistry 32, 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
  • 19
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Wright, P.E. & Jennings, P.A. (1993). Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-895.
    • (1993) Science , vol.262 , pp. 892-895
    • Wright, P.E.1    Jennings, P.A.2
  • 21
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • Itzhaki, L.S., Otzen, D.E. & Fersht, A.R. (1995). The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J. Mol. Biol. 254, 260-288.
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 22
    • 0030334834 scopus 로고    scopus 로고
    • Structure of the transition state for folding of the 1 29 amino acid protein CheY resembles that of a smaller protein, Cl-2
    • López-Hernández, E. & Serrano, L. (1996). Structure of the transition state for folding of the 1 29 amino acid protein CheY resembles that of a smaller protein, Cl-2. Fold. Des. 1, 43-55.
    • (1996) Fold. Des. , vol.1 , pp. 43-55
    • López-Hernández, E.1    Serrano, L.2
  • 24
    • 36449002968 scopus 로고
    • Energy landscapes, glass transitions and chemical reaction dynamics in biomolecular or solvent environment
    • Onuchic, J.N. & Wolynes, P.G. (1993). Energy landscapes, glass transitions and chemical reaction dynamics in biomolecular or solvent environment. J. Chem. Phys. 98, 2218-2224.
    • (1993) J. Chem. Phys. , vol.98 , pp. 2218-2224
    • Onuchic, J.N.1    Wolynes, P.G.2
  • 25
    • 21144473420 scopus 로고
    • Electron transfer reactions in chemistry: Theory and experiment
    • Marcus, R.A. (1993). Electron transfer reactions in chemistry: theory and experiment. Rev. Mod. Phys. 65, 599-610.
    • (1993) Rev. Mod. Phys. , vol.65 , pp. 599-610
    • Marcus, R.A.1
  • 26
    • 0001861319 scopus 로고
    • How to fold graciously
    • (DeBrunner, P., Tsibris, J. & Munck, E., eds), University of Illinois Press, Urbana, IL
    • Levinthal, C. (1969). How to fold graciously. In Mossbauer Spectroscopy in Biological Systems. (DeBrunner, P., Tsibris, J. & Munck, E., eds), pp. 22-24, University of Illinois Press, Urbana, IL.
    • (1969) Mossbauer Spectroscopy in Biological Systems , pp. 22-24
    • Levinthal, C.1
  • 27
    • 0024733407 scopus 로고
    • Intermediates and barrier crossing in a random energy model (with applications to protein folding)
    • Bryngelson, J.D. & Wolynes, P.G. (1989). Intermediates and barrier crossing in a random energy model (with applications to protein folding). J. Phys. Chem. 93, 6902-6915.
    • (1989) J. Phys. Chem. , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 28
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • Bryngelson, J.D. & Wolynes, P.G. (1987). Spin glasses and the statistical mechanics of protein folding. Proc. Natl. Acad. Sci. USA 84, 7524-7528.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 29
    • 0026723063 scopus 로고
    • Protein folding funnels: A kinetic approach to the sequence-structure relationship
    • Leopold, P.E., Montai, M. & Onuchic, J.N. (1992). Protein folding funnels: a kinetic approach to the sequence-structure relationship. Proc. Natl. Acad. USA 89, 8721-8725.
    • (1992) Proc. Natl. Acad. USA , vol.89 , pp. 8721-8725
    • Leopold, P.E.1    Montai, M.2    Onuchic, J.N.3
  • 31
    • 0000710672 scopus 로고    scopus 로고
    • Diffusive dynamics of the reaction coordinate for protein folding funnels
    • Socci, N.D., Onuchic, J.N. & Wolynes, P.G. (1996). Diffusive dynamics of the reaction coordinate for protein folding funnels. J. Chem. Phys. 104, 5860-5868.
    • (1996) J. Chem. Phys. , vol.104 , pp. 5860-5868
    • Socci, N.D.1    Onuchic, J.N.2    Wolynes, P.G.3
  • 32
    • 0001143109 scopus 로고
    • Helix-coil, liquid-crystal and spin-glass transitions of a collapsed heteropolymer
    • Luthey-Schulten, Z.A., Ramirez, B.E. & Wolynes, P.G. (1995). Helix-coil, liquid-crystal and spin-glass transitions of a collapsed heteropolymer. J. Phys. Chem. 99, 2177-2185.
    • (1995) J. Phys. Chem. , vol.99 , pp. 2177-2185
    • Luthey-Schulten, Z.A.1    Ramirez, B.E.2    Wolynes, P.G.3
  • 34
    • 0029964867 scopus 로고    scopus 로고
    • Diffusion limited contact formation in unfolded cytochrome c: Estimating the maximum rate of protein folding
    • in press
    • Hagen, S.J., Hofrichter, J., Szabo, A. & Eaton, W.A. (1996). Diffusion limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding. Proc. Natl. Acad. Sci., in press.
    • (1996) Proc. Natl. Acad. Sci.
    • Hagen, S.J.1    Hofrichter, J.2    Szabo, A.3    Eaton, W.A.4
  • 37
    • 0026694167 scopus 로고
    • A model of the molten globule state from molecular dynamics simulations
    • Daggett, V. & Levitt, M. (1992). A model of the molten globule state from molecular dynamics simulations. Proc. Natl. Acad. Sci. USA 89, 5142-5146.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5142-5146
    • Daggett, V.1    Levitt, M.2
  • 38
    • 0030165480 scopus 로고    scopus 로고
    • A correlated energy landscape model for finite, random heteropolymers
    • in press
    • Plotkin, S.S., Wang, J. & Wolynes, P.G. (1996). A correlated energy landscape model for finite, random heteropolymers. Phys. Rev. E, in press.
    • (1996) Phys. Rev. E
    • Plotkin, S.S.1    Wang, J.2    Wolynes, P.G.3


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